SitesBLAST

G85 (= G12) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T14) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
L101 (vs. gap) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
K102 (vs. gap) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
C109 (≠ A34) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P39) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
K119 (= K44) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ G50) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
M126 (≠ I51) to V: in CBSD; loss of activity
E131 (≠ I56) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G64) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ V68) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E69) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G73) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N74) binding pyridoxal 5'-phosphate
L154 (= L79) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A80) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
C165 (≠ T90) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
M173 (≠ Q98) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
E176 (= E101) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
V180 (≠ M105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ V116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ A135) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ V155) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N157) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
A231 (= A160) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (= D163) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
GTGGT 256:260 (= GTGGT 185:189) binding pyridoxal 5'-phosphate
T257 (= T186) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ A191) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
R266 (≠ M195) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K198) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ N201) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ V204) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
I278 (≠ A207) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
D281 (= D210) to N: in CBSD; loss of activity
A288 (≠ Y217) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ S231) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
G305 (= G235) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G237) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
V320 (= V250) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D251) to V: in CBSD; loss of activity
R336 (≠ F266) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
L338 (= L268) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
G347 (= G277) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S279) binding pyridoxal 5'-phosphate; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
T353 (≠ N283) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ T299) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D306) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ T309) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
K384 (= K314) to E: in CBSD; severe form; dbSNP:rs121964967

Sites not aligning to the query:

18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
52 binding axial binding residue
58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
69 A → P: in dbSNP:rs17849313
78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989

1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
39% identity, 93% coverage: 7:324/343 of query aligns to 38:345/348 of 1jbqA

query
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active site: K77 (= K44), S105 (≠ A72), D232 (= D210), S236 (≠ A214), L238 (= L216), S300 (= S279), P326 (≠ C305)
binding protoporphyrin ix containing fe: A177 (≠ V155), P180 (≠ R158), L181 (≠ Q159), Y184 (≠ I162), R217 (≠ M195)
binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), V206 (= V184), G207 (= G185), T208 (= T186), G209 (= G187), G210 (= G188), T211 (= T189), G256 (= G235), S300 (= S279), P326 (≠ C305), D327 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 9, 10, 11, 12, 16, 20, 21, 22, 23

P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
39% identity, 94% coverage: 1:324/343 of query aligns to 1:320/464 of P9WP51

query
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P9WP51

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Sites not aligning to the query:

428 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
40% identity, 92% coverage: 9:324/343 of query aligns to 7:318/458 of 7xoyA

query
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7xoyA

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S

V

V

S

S

G

D

R

R

L

L

A

V

Q

R

E

D

I

I

A

-

K

-

T

-

A

-

P

-

H

D

G

G

A

A

I

W

W

K

A

P

N

D

Q

Q

F

Y

D

A

N

N

V

P

A

E

N

G

R

P

Q

A

A

S

H

H

I

Y

D

V

T

T

G

G

P

P

E

E

I

I

W

W

D

A

Q

D

T

T

D

E

G

G

K

K

V

V

D

T

G

H

F

F

V

V

S

A

A

G

V

I

G

G

T
|
T

G

G

G
|
G

T
|
T

F

I

A

T

G

G

V

A

G

G

M

R

A

Y

L

L

K

K

-

E

A

V

R

S

N

G

K

G

D

R

V

V

K

R

I

I

A

V

L

G

A

A

D

D

P

P

L

E

G

G

A

-

L

-

Y

-

S

S

Y

V

Y

Y

T

S

T

G

G

G

E

-

L

-

K

-

A

A

E

G

G

R

S

P

S

Y

I

L

T

V

E

E

G

G

I

V

G

G

Q

E

G

D

R

F

I

W

T

P

A

A

N

A

L

Y

E

D

D

P

A

S

P

V

V

P

D

D

H

E

A

I

F

I

Q

A

I

V

T

S

D

D

E

S

E

D

A

S

V

F

P

D

I

M

V

T

F

R

D

R

L

L

L

A

E

R

H

E

E

E

G

A

L

M

C

L

L

V

G

G

S
|
S

S

C

G

G

I

M

N

A

I

V

A

V

G

A

A

A

I

L

R

K

L

V

A

A

K

E

E

E

L

A

G

G

P

P

G

D

H

A

T

L

I

I

V

V

T

V

I

L

L

L

C
x
P

D

D

Y

G

G

G

T

R

R

G

Y

Y

Q

M

S

S

K

K

L

I

F

F

N

N

P

D

-

A

-

W

-

M

-

S

-

Y

D

G

F

F

L

L

R

R

S

S

K

R

binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: K42 (= K44), S70 (≠ A72), N72 (= N74), T73 (= T75), T180 (= T186), G182 (= G188), T183 (= T189), S267 (= S279), P293 (≠ C305)

7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
40% identity, 92% coverage: 9:324/343 of query aligns to 7:318/458 of 7xnzB

query
sites
7xnzB

E

E

S

L

I

I

G

G

N

G

T

T

P

P

L

L

I

V

K

R

L

L

K

N

K

S

A

V

S

V

E

P

L

D

T

G

G

A

C

G

T

T

I

V

L

A

G

A

K

K

A

V

E

E

F

Y

M

L

N

N

P

P

G

G

Q

G

S

S

V

S

K
|
K

D

D

R

R

A

I

A

A

L

V

G

K

I

M

I

I

R

E

D

A

A

A

I

E

A

A

K

S

K

G

Q

Q

I

L

E

K

P

P

G

G

V

T

I

I

V

V

E

E

G

P

T

T

A

S

G

G

N

N

T

T

G

G

I

V

G

G

L

L

A

A

L

L

V

V

A

A

A

Q

P

R

F

R

G

G

F

Y

K

K

T

C

V

V

I

F

V

V

I

C

P

P

E

D

T

K

Q

V

S

S

Q

E

E

D

K

K

K

R

D

N

M

V

L

L

R

I

L

A

A

Y

G

G

A

A

T

E

L

V

V

V

E

V

V

C

P

P

-

T

A

A

V

V

A

P

Y

P

A

H

N

D

P

P

N

A

N

S

Y

Y

V

Y

K

S

V

V

S

S

G

D

R

R

L

L

A

V

Q

R

E

D

I

I

A

-

K

-

T

-

A

-

P

-

H

D

G

G

A

A

I

W

W

K

A

P

N

D

Q

Q

F

Y

D

A

N

N

V

P

A

E

N

G

R

P

Q

A

A

S

H

H

I

Y

D

V

T

T

G

G

P

P

E

E

I

I

W

W

D

A

Q

D

T

T

D

E

G

G

K

K

V

V

D

T

G

H

F

F

V

V

S

A

A

G

V

I

G
|
G

T
|
T

G
|
G

T
|
T

F

I

A

T

G

G

V

A

G

G

M

R

A

Y

L

L

K

K

-

E

A

V

R

S

N

G

K

G

D

R

V

V

K

R

I

I

A

V

L

G

A

A

D

D

P

P

L

E

G

G

A

-

L

-

Y

-

S

S

Y

V

Y

Y

T

S

T

G

G

G

E

-

L

-

K

-

A

A

E

G

G

R

S

P

S

Y

I

L

T

V

E

E

G

G

I

V

G

G

Q

E

G

D

R

F

I

W

T

P

A

A

N

A

L

Y

E

D

D

P

A

S

P

V

V

P

D

D

H

E

A

I

F

I

Q

A

I

V

T

S

D

D

E

S

E

D

A

S

V

F

P

D

I

M

V

T

F

R

D

R

L

L

L

A

E

R

H

E

E

E

G

A

L

M

C

L

L

V

G

G

S
|
S

S

C

G

G

I

M

N

A

I

V

A

V

G

A

A

A

I

L

R

K

L

V

A

A

K

E

E

E

L

A

G

G

P

P

G

D

H

A

T

L

I

I

V

V

T

V

I

L

L

L

C
x
P

D
|
D

Y

G

G

G

T

R

R

G

Y

Y

Q

M

S

S

K

K

L

I

F

F

N

N

P

D

-

A

-

W

-

M

-

S

-

Y

D

G

F

F

L

L

R

R

S

S

K

R

binding pyridoxal-5'-phosphate: K42 (= K44), G179 (= G185), T180 (= T186), G181 (= G187), G182 (= G188), T183 (= T189), S267 (= S279), P293 (≠ C305), D294 (= D306)

6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
34% identity, 92% coverage: 5:321/343 of query aligns to 10:324/468 of 6xylA

query
sites
6xylA

D

D

G

S

L

V

V

L

E

D

S

A

I

I

G

G

N

N

T

T

P

P

L

M

I

V

K

R

L

M

K

K

K

R

A

L

S

A

E

K

L

V

T

Y

G

G

-

L

-

E

C

C

T

D

I

L

L

L

G

A

K

K

A

C

E

E

F

F

M

M

N

S

P

A

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

K

G

A

I

M

I

V

R

E

D

K

A

A

I

E

A

R

K

E

K

G

Q

R

I

L

E

K

P

A

G

G

G

D

V

T

I

L

V

I

E

E

G

P

T

T

A

S

G

G

N

N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

L

V

A

A

A

P

V

F

R

G

G

F

Y

K

R

T

M

V

I

I

V

V

T

I

M

P

P

E

A

T

K

Q

M

S

S

Q

A

E

E

K

K

K

S

D

N

M

I

L

M

R

K

L

C

A

L

G

G

A

A

T

E

L

I

V

V

E

R

V

T

P

P

A

T

-

E

V

A

A

A

Y

W

A

N

N

D

P

E

N

N

N

S

Y

H

V

M

K

G

V

V

S

A

G

A

R

K

L

L

A

Q

Q

R

E

E

I

L

A

-

K

-

T

-

A

-

P

-

H

E

G

N

A

A

I

H

W

I

A

L

N

D

Q
|
Q

F

Y

D

N

N

N

V

T

A

A

N

N

R

P

Q

M

A

V

H

H

I

Y

D

D

T

V

T

T

G

A

P

E

E

E

I

I

W

I

D

T

Q

Q

T

C

D

D

G

G

K

D

V

I

D

D

G

M

F

V

V

V

S

I

A

G

V

A

G
|
G

T
|
T

G
|
G

G

G

T
|
T

F

I

A

T

G

G

V

I

G

G

M

R

A

K

L

I

K

K

A

E

R

R

N

C

K

P

D

K

V

C

K

K

I

V

A

V

L

G

A

V

D

D

P

P

L

K

G

G

A

S

A

I

L

L

Y

A

S

V

Y

P

Y

D

T

S

T

L

G

N

E

D

L

E

K

K

A

R

E

L

G

Q

S

S

S

Y

I

E

T

V

E

E

G
|
G

I
|
I

G

G

Q
x
Y

G

D

R

F

I

V

T

P

A

G

N

V

L

L

E

D

D

R

A

K

P

V

V

V

D

D

H

E

A

W

F

V

Q

K

I

V

T

G

D

D

E

A

E

E

A

S

V

F

P

T

I

T

V

A

F

R

D

A

L

I

E

R

H

N

E

E

G

G

L

L

C

F

L

V

G

G

S
|
S

S

S

G

G

I

A

N

N

I

V

A

W

G

G

A

A

I

L

R

Q

L

A

A

A

K

R

E

Q

L

L

G

K

P

K

G

G

H

Q

T

K

I

C

V

V

T

V

I

L

L

L

C
x
P

D
|
D

Y

S

G

S

T

R

R

N

Y

Y

Q

M

S

S

K

K

L

F

F

I

N

S

P

D

D

E

F

W

L

M

binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K44), T82 (= T75), Q154 (= Q151), G188 (= G185), T189 (= T186), G190 (= G187), T192 (= T189), G238 (= G235), I239 (= I236), Y241 (≠ Q238), S282 (= S279), P308 (≠ C305), D309 (= D306)

6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
34% identity, 92% coverage: 5:321/343 of query aligns to 10:324/477 of 6xwlC

query
sites
6xwlC

D

D

G

S

L

V

V

L

E

D

S

A

I

I

G

G

N

N

T

T

P

P

L

M

I

V

K

R

L

M

K

K

K

R

A

L

S

A

E

K

L

V

T

Y

G

G

-

L

-

E

C

C

T

D

I

L

L

L

G

A

K

K

A

C

E

E

F

F

M

M

N

S

P

A

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

K

G

A

I

M

I

V

R

E

D

K

A

A

I

E

A

R

K

E

K

G

Q

R

I

L

E

K

P

A

G

G

G

D

V

T

I

L

V

I

E

E

G

P

T

T

A

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

L

L

V

A

A

A

P

V

F

R

G

G

F

Y

K

R

T

M

V

I

I

V

V

T

I

M

P

P

E

A

T

K

Q

M

S

S

Q

A

E

E

K

K

K

S

D

N

M

I

L

M

R

K

L

C

A

L

G

G

A

A

T

E

L

I

V

V

E

R

V

T

P

P

A

T

-

E

V

A

A

A

Y

W

A

N

N

D

P

E

N

N

N

S

Y

H

V

M

K

G

V

V

S

A

G

A

R

K

L

L

A

Q

Q

R

E

E

I

L

A

-

K

-

T

-

A

-

P

-

H

E

G

N

A

A

I

H

W

I

A

L

N

D

Q

Q

F

Y

D

N

N

N

V

T

A

A

N

N

R

P

Q

M

A

V

H

H

I

Y

D

D

T

V

T

T

G

A

P

E

E

E

I

I

W

I

D

T

Q

Q

T

C

D

D

G

G

K

D

V

I

D

D

G

M

F

V

V

V

S

I

A

G

V

A

G
|
G

T
|
T

G
|
G

G

G

T
|
T

F

I

A

T

G

G

V

I

G

G

M

R

A

K

L

I

K

K

A

E

R

R

N

C

K

P

D

K

V

C

K

K

I

V

A

V

L

G

A

V

D

D

P

P

L

K

G

G

A

S

A

I

L

L

Y

A

S

V

Y

P

Y

D

T

S

T

L

G

N

E

D

L

E

K

K

A

R

E

L

G

Q

S

S

S

Y

I

E

T

V

E

E

G
|
G

I

I

G

G

Q

Y

G

D

R

F

I

V

T

P

A

G

N

V

L

L

E

D

D

R

A

K

P

V

V

V

D

D

H

E

A

W

F

V

Q

K

I

V

T

G

D

D

E

A

E

E

A

S

V

F

P

T

I

T

V

A

F

R

D

A

L

I

E

R

H

N

E

E

G

G

L

L

C

F

L

V

G

G

S
|
S

S

S

G

G

I

A

N

N

I

V

A

W

G

G

A

A

I

L

R

Q

L

A

A

A

K

R

E

Q

L

L

G

K

P

K

G

G

H

Q

T

K

I

C

V

V

T

V

I

L

L

L

C
x
P

D
|
D

Y

S

G

S

T

R

R

N

Y

Y

Q

M

S

S

K

K

L

F

F

I

N

S

P

D

D

E

F

W

L

M

binding pyridoxal-5'-phosphate: K51 (= K44), N81 (= N74), G188 (= G185), T189 (= T186), G190 (= G187), T192 (= T189), G238 (= G235), S282 (= S279), P308 (≠ C305), D309 (= D306)

6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
33% identity, 94% coverage: 4:326/343 of query aligns to 7:335/344 of 6c4pA

query
sites
6c4pA

R

R

D

H

G

N

L

V

V

I

E

D

S

L

I

V

G

G

N

N

T

T

P

P

L

L

I

I

K

A

L

L

K

K

A

L

S

P

E

K

L

A

T

L

G

G

C

I

T

K

-

P

-

Q

I

I

L

Y

G

A

K

K

A

L

E

E

F

L

M

Y

N

N

P

P

G

G

Q

G

S

S

V

I

K
|
K

D

D

R

R

A

I

A

A

L

K

G

S

I

M

I

V

R

E

D

E

A

A

I

E

A

A

K

S

K

G

Q

R

I

I

E

H

P

P

G

S

-

R

G

S

V

T

I

L

V

I

E

E

G

P

T

T

A

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

L

L

V

I

A

G

A

A

P

I

F

K

G

G

F

Y

K

R

T

T

V

I

I

I

V

T

I

L

P

P

E

E

T

K

Q

M

S

S

Q

N

E

E

K

K

K

V

D

S

M

V

L

L

R

K

L

A

A

L

G

G

A

A

T

E

L

I

V

I

E

R

V

T

P

P

-

T

A

A

V

A

A

A

Y

W

A

D

N

S

P

P

N

E

N

S

Y

H

V

I

K

G

V

V

S

A

G

K

R

K

L

L

A

E

Q

K

E

E

I

I

A

P

K

-

T

-

A

-

P

-

H

-

G

G

A

A

I

V

W

I

A

L

N

D

Q

Q

F

Y

D

N

N

N

V

M

A

M

N

N

R

P

Q

E

A

A

H

H

I

Y

D

F

T

G

T

T

G

G

P

R

E

E

I

I

W

Q

D

R

Q

Q

T

L

D

E

-

D

-

L

-
x
N

-

L

-

F

G
x
D

K
x
N

V

L

D

R

G

A

F

V

V

V

S

A

A

G

V
x
A

G
|
G

T
|
T

G
|
G

G

G

T
|
T

F

I

A

S

G

G

V

I

G

S

M

K

A

Y

L

L

K

K

A

E

R

Q

N

N

K

D

D

K

V

I

K

Q

I

I

A

V

L

G

A

A

D

D

P

P

L

F

G

G

A

S

A

I

L

L

Y

A

S

Q

Y

P

Y

E

T

N

T

L

G

N

E

K

L

T

K

D

A

I

E

T

G

D

S

Y

S

K

I

V

T

-

E

E

G
|
G

I

I

G

G

Q

Y

G

D

R

F

I

V

T

P

A

Q

N

V

L

L

E

D

D

R

A

K

P

L

V

I

D

D

H

V

A

W

F

Y

Q

K

I

T

T

D

D

D

E

K

E

P

A

S

V

F

P

K

I

Y

V

A

F

R

D

Q

L

L

L

I

E

S

H

N

E

E

G

G

L

V

C

L

L

V

G

G

S
|
S

S

S

G

G

I

S

N

A

I

F

A

T

G

A

A

V

I

V

R

K

L

Y

A

C

K

E

-

D

-

H

-

P

E

E

L

L

G

T

P

E

G

D

H

D

T

V

I

I

V

V

T

A

I

I

L

F

C
x
P

D
|
D

Y

S

G

I

T

R

R

S

Y

Y

Q

L

S

T

K

K

L

F

F

V

N

D

P

D

D

E

F

W

L

L

R

K

S

K

K

N

N

N

L

L

binding calcium ion: N179 (vs. gap), D182 (≠ G175), N183 (≠ K176)
binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K44), N80 (= N74), A191 (≠ V184), G192 (= G185), T193 (= T186), G194 (= G187), T196 (= T189), G241 (= G235), S285 (= S279), P314 (≠ C305), D315 (= D306)

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
38% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2efyA

query
sites
2efyA

S

A

I

I

G

G

N

K

T

T

P

P

L

V

I

V

K

R

L

L

K

A

K

K

A

V

S

V

E

E

L

P

T

D

G

M

C

A

T

E

I

V

L

W

G

V

K

K

A

L

E

E

F

G

M

L

N

N

P

P

G

G

Q

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

G

Y

I

M

I

I

R

K

D

D

A

A

I

E

A

E

K

R

K

G

Q

I

I

L

E

R

P

P

G

G

G

S

-

G

-

Q

V

V

I

I

V

V

E

E

G

P

T
|
T

A
x
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

M

V

I

A

A

P

S

F

R

G

G

F

Y

K

R

T

L

V

I

I

L

V

T

I

M

P

P

E

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

K

K

D

R

M

V

L

L

R

K

L

A

A

F

G

G

A

A

T

E

L

L

V

V

E

-

V

-

P

-

A

-

V

-

A

-

Y

L

A

T

N

D

P

P

N

E

N

R

Y

R

V

M

K

L

V

A

S

A

G

R

-

E

-

A

-

L

R

R

L

L

A

K

Q

E

E

E

I

L

A

-

K

-

T

-

A

-

P

-

H

-

G

G

A

A

I

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

V

P

A

A

N

N

R

V

Q

R

A

A

H

H

I

Y

D

E

T

T

G

G

P

P

E

E

I

L

W

Y

D

E

Q

A

T

L

D

E

G

G

K

R

V

I

D

D

G

A

F

F

V

V

S
x
Y

A

G

V

S

G
|
G

T
|
T

G
|
G

G

G

T
|
T

F

I

A

T

G

G

V

V

G

G

M

R

A

Y

L

L

K

K

A

E

R

R

N

I

K

P

D

H

V

V

K

K

I

V

A

I

L

A

A

V

D
x
E

P

P

L

-

G

-

A

-

A

A

L

R

Y
x
S

S

N

Y

V

Y

L

T

S

T

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

-

I

-

T

F

E

Q

G
|
G

I
x
M

G

G

Q
x
P

G

G

R

F

I

I

T

P

A

E

N

N

L

L

E

D

D

L

A

S

P

L

V

L

D

D

H

G

A

V

F

I

Q

Q

I

V

T

W

D

E

E

E

E

D

A

A

V

F

P

P

I

L

V

A

F

R

D

R

L

L

L

A

E

R

H

E

E

E

G

G

L

L

C

F

L

L

G

G

G

M

S
|
S

S

S

G

G

I

G

N

I

I

V

A

W

G

A

A

A

I

L

R

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

H

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D
|
D

Y

G

G

G

T

W

R

K

Y

Y

Q

L

S

S

active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
binding 5-oxohexanoic acid: T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q151), G175 (= G185), G219 (= G235), M220 (≠ I236), P222 (≠ Q238)
binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G175 (= G185), T176 (= T186), G177 (= G187), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305), D290 (= D306)

2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
38% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2ecqA

query
sites
2ecqA

S

A

I

I

G

G

N

K

T

T

P

P

L

V

I

V

K

R

L

L

K

A

K

K

A

V

S

V

E

E

L

P

T

D

G

M

C

A

T

E

I

V

L

W

G

V

K

K

A

L

E

E

F

G

M

L

N

N

P

P

G

G

Q

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

G

Y

I

M

I

I

R

K

D

D

A

A

I

E

A

E

K

R

K

G

Q

I

I

L

E

R

P

P

G

G

G

S

-

G

-

Q

V

V

I

I

V

V

E

E

G

P

T

T

A
x
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

M

V

I

A

A

P

S

F

R

G

G

F

Y

K

R

T

L

V

I

I

L

V

T

I

M

P

P

E

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

K

K

D

R

M

V

L

L

R

K

L

A

A

F

G

G

A

A

T

E

L

L

V

V

E

-

V

-

P

-

A

-

V

-

A

-

Y

L

A

T

N

D

P

P

N

E

N

R

Y

R

V

M

K

L

V

A

S

A

G

R

-

E

-

A

-

L

R

R

L

L

A

K

Q

E

E

E

I

L

A

-

K

-

T

-

A

-

P

-

H

-

G

G

A

A

I

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

V

P

A

A

N

N

R

V

Q

R

A

A

H

H

I

Y

D

E

T

T

G

G

P

P

E

E

I

L

W

Y

D

E

Q

A

T

L

D

E

G

G

K

R

V

I

D

D

G

A

F

F

V

V

S
x
Y

A
x
G

V

S

G
|
G

T
|
T

G

G

T
|
T

F

I

A

T

G

G

V

V

G

G

M

R

A

Y

L

L

K

K

A

E

R

R

N

I

K

P

D

H

V

V

K

K

I

V

A

I

L

A

A

V

D
x
E

P

P

L

-

G

-

A

-

A

A

L

R

Y
x
S

S

N

Y

V

Y

L

T

S

T

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

-

I

-

T

F

E

Q

G
|
G

I

M

G

G

Q

P

G

G

R

F

I

I

T

P

A

E

N

N

L

L

E

D

D

L

A

S

P

L

V

L

D

D

H

G

A

V

F

I

Q

Q

I

V

T

W

D

E

E

E

E

D

A

A

V

F

P

P

I

L

V

A

F

R

D

R

L

L

L

A

E

R

H

E

E

E

G

G

L

L

C

F

L

L

G

G

G

M

S
|
S

S

S

G

G

I

G

N

I

I

V

A

W

G

A

A

A

I

L

R

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

H

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D

D

Y

G

G

G

T

W

R

K

Y

Y

Q

L

S

S

active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
binding (3s)-3-hydroxybutanoic acid: K40 (= K44), G71 (= G73), T73 (= T75), Q141 (= Q151), G219 (= G235)
binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G173 (≠ A183), G175 (= G185), T176 (= T186), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305)

2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
38% identity, 89% coverage: 10:313/343 of query aligns to 6:297/302 of 2ecoA

query
sites
2ecoA

S

A

I

I

G

G

N

K

T

T

P

P

L

V

I

V

K

R

L

L

K

A

K

K

A

V

S

V

E

E

L

P

T

D

G

M

C

A

T

E

I

V

L

W

G

V

K

K

A

L

E

E

F

G

M

L

N

N

P

P

G

G

Q

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

G

Y

I

M

I

I

R

K

D

D

A

A

I

E

A

E

K

R

K

G

Q

I

I

L

E

R

P

P

G

G

G

S

-

G

-

Q

V

V

I

I

V

V

E

E

G

P

T
|
T

A
x
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

M

V

I

A

A

P

S

F

R

G

G

F

Y

K

R

T

L

V

I

I

L

V

T

I

M

P

P

E

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

K

K

D

R

M

V

L

L

R

K

L

A

A

F

G

G

A

A

T

E

L

L

V

V

E

-

V

-

P

-

A

-

V

-

A

-

Y

L

A

T

N

D

P

P

N

E

N

R

Y

R

V

M

K

L

V

A

S

A

G

R

-

E

-

A

-

L

R

R

L

L

A

K

Q

E

E

E

I

L

A

-

K

-

T

-

A

-

P

-

H

-

G

G

A

A

I

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

V

P

A

A

N

N

R

V

Q

R

A

A

H

H

I

Y

D

E

T

T

G

G

P

P

E

E

I

L

W

Y

D

E

Q

A

T

L

D

E

G

G

K

R

V

I

D

D

G

A

F

F

V

V

S
x
Y

A

G

V

S

G
|
G

T
|
T

G

G

T
|
T

F

I

A

T

G

G

V

V

G

G

M

R

A

Y

L

L

K

K

A

E

R

R

N

I

K

P

D

H

V

V

K

K

I

V

A

I

L

A

A

V

D
x
E

P

P

L

-

G

-

A

-

A

A

L

R

Y
x
S

S

N

Y

V

Y

L

T

S

T

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

-

I

-

T

F

E

Q

G
|
G

I

M

G

G

Q

P

G

G

R

F

I

I

T

P

A

E

N

N

L

L

E

D

D

L

A

S

P

L

V

L

D

D

H

G

A

V

F

I

Q

Q

I

V

T

W

D

E

E

E

E

D

A

A

V

F

P

P

I

L

V

A

F

R

D

R

L

L

L

A

E

R

H

E

E

E

G

G

L

L

C

F

L

L

G

G

G

M

S
|
S

S

S

G

G

I

G

N

I

I

V

A

W

G

A

A

A

I

L

R

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

H

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D
|
D

Y

G

G

G

T

W

R

K

Y

Y

Q

L

S

S

active site: K40 (= K44), S70 (≠ A72), E200 (≠ D210), S204 (≠ Y217), S263 (= S279)
binding 4-methyl valeric acid: K40 (= K44), T69 (= T71), G71 (= G73), T73 (= T75), Q141 (= Q151), G175 (= G185), T176 (= T186), G219 (= G235)
binding pyridoxal-5'-phosphate: K40 (= K44), N72 (= N74), Y172 (≠ S182), G175 (= G185), T176 (= T186), T179 (= T189), G219 (= G235), S263 (= S279), P289 (≠ C305), D290 (= D306)

3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
36% identity, 94% coverage: 7:329/343 of query aligns to 41:360/500 of 3pc2A

query
sites
3pc2A

L

I

V

L

E

E

S

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

K

K

L

L

K

N

-

I

-

P

A

A

S

S

E

D

L

G

T

I

G

E

C

C

T

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

M

L

N

N

P

P

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

G

R

I

M

I

V

R

Q

D

D

A

A

I

E

A

E

K

Q

K

G

Q

L

I

L

E

K

P

P

G

G

G

Y

V

T

I

I

V

I

E

E

G

P

T

T

A

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

L

M

V

A

A

C

A

A

P

V

F

K

G

G

F

Y

K

K

T

C

V

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

S

S

Q

N

E

E

K

K

K

V

D

S

M

A

L

L

R

R

L

T

A

L

G

G

A

A

T

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

A

A

Y

Y

A

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

V

V

S

-

G

-

R

-

L

-

A

A

Q

Q

E

Q

I

L

A

Q

K

R

T

E

A

T

P

P

H

N

G

-

A

S

I

I

W

V

A

L

N

D

Q

Q

F

Y

D

R

N

N

V
x
A

A

G

N

N

R
x
P

Q
x
L

A

A

H

H

I
x
Y

D

D

T

G

T

T

G

A

P

A

E

E

I

I

W

L

D

W

Q

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

V

V

S

V

A

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

F

I

A

S

G

G

V

I

G

G

M
x
R

A

K

L

I

K

K

A

E

R

Q

N

V

K

P

D

S

V

C

K

Q

I

I

A

V

L

G

A

V

D

D

P

P

L

Y

G

G

A

S

A

I

L

L

Y

A

S

R

Y

P

Y

A

T

E

T

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

I

V

T

-

E

E

G
|
G

I

I

G

G

Q

Y

G

D

R

F

I

P

T

P

A

T

N

V

L

F

E

D

D

D

A

T

P

V

V

V

D

D

H

V

A

W

F

T

Q

K

I

I

T

G

D

D

E

S

E

D

A

C

V

F

P

P

I

M

V

S

F

R

D

R

L

L

L

N

E

A

H

E

E

E

G

G

L

L

C

L

L

C

G

G

S
|
S

S

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

I

L

R

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

Y

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

V

N

S

P

D

D

N

F

W

L

M

R

E

S

A

K

R

N

N

L

F

P

K

V

E

P

P

active site: K80 (= K44), S310 (= S279)
binding protoporphyrin ix containing fe: A187 (≠ V155), P190 (≠ R158), L191 (≠ Q159), Y194 (≠ I162), R227 (≠ M195)
binding pyridoxal-5'-phosphate: K80 (= K44), N110 (= N74), A216 (≠ V184), G217 (= G185), T218 (= T186), A219 (≠ G187), T221 (= T189), G266 (= G235), S310 (= S279), P336 (≠ C305), D337 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 12, 13, 14, 15, 16, 24, 25, 26

3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
36% identity, 94% coverage: 7:329/343 of query aligns to 43:362/504 of 3pc4A

query
sites
3pc4A

L

I

V

L

E

E

S

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

K

K

L

L

K

N

-

I

-

P

A

A

S

S

E

D

L

G

T

I

G

E

C

C

T

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

M

L

N

N

P

P

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

G

R

I

M

I

V

R

Q

D

D

A

A

I

E

A

E

K

Q

K

G

Q

L

I

L

E

K

P

P

G

G

G

Y

V

T

I

I

V

I

E

E

G

P

T
|
T

A
x
S

G

G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

M

V

A

A

C

A

A

P

V

F

K

G

G

F

Y

K

K

T

C

V

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

S

S

Q

N

E

E

K

K

K

V

D

S

M

A

L

L

R

R

L

T

A

L

G

G

A

A

T

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

A

A

Y

Y

A

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

V

V

S

-

G

-

R

-

L

-

A

A

Q

Q

E

Q

I

L

A

Q

K

R

T

E

A

T

P

P

H

N

G

-

A

S

I

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

V
x
A

A

G

N

N

R
x
P

Q
x
L

A

A

H

H

I
x
Y

D

D

T

G

T

T

G

A

P

A

E

E

I

I

W

L

D

W

Q

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

V

V

S

V

A

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

F

I

A

S

G

G

V

I

G

G

M
x
R

A

K

L

I

K

K

A

E

R

Q

N

V

K

P

D

S

V

C

K

Q

I

I

A

V

L

G

A

V

D

D

P

P

L

Y

G

G

A

S

A

I

L

L

Y

A

S

R

Y

P

Y

A

T

E

T

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

I

V

T

-

E

E

G
|
G

I
|
I

G

G

Q
x
Y

G

D

R

F

I

P

T

P

A
x
T

N

V

L

F

E

D

D

D

A

T

P

V

V

V

D

D

H

V

A

W

F

T

Q

K

I

I

T

G

D

D

E

S

E

D

A

C

V

F

P

P

I

M

V

S

F

R

D

R

L

L

L

N

E

A

H

E

E

E

G

G

L

L

C

L

L

C

G

G

S
|
S

S

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

I

L

R

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

Y

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

V

N

S

P

D

D

N

F

W

L

M

R

E

S

A

K

R

N

N

L

F

P

K

V

E

P

P

active site: K82 (= K44), S312 (= S279)
binding protoporphyrin ix containing fe: A189 (≠ V155), P192 (≠ R158), L193 (≠ Q159), Y196 (≠ I162), R229 (≠ M195), T276 (≠ A243)
binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q151), A218 (≠ V184), G219 (= G185), T220 (= T186), A221 (≠ G187), T223 (= T189), G268 (= G235), I269 (= I236), Y271 (≠ Q238), S312 (= S279), P338 (≠ C305), D339 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 14, 15, 16, 17, 18, 26, 27, 28

3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
36% identity, 94% coverage: 7:329/343 of query aligns to 43:362/504 of 3pc3A

query
sites
3pc3A

L

I

V

L

E

E

S

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

K

K

L

L

K

N

-

I

-

P

A

A

S

S

E

D

L

G

T

I

G

E

C

C

T

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

M

L

N

N

P

P

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

G

R

I

M

I

V

R

Q

D

D

A

A

I

E

A

E

K

Q

K

G

Q

L

I

L

E

K

P

P

G

G

G

Y

V

T

I

I

V

I

E

E

G

P

T
|
T

A
x
S

G

G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

L

M

V

A

A

C

A

A

P

V

F

K

G

G

F

Y

K

K

T

C

V

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

S

S

Q

N

E

E

K

K

K

V

D

S

M

A

L

L

R

R

L

T

A

L

G

G

A

A

T

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

A

A

Y

Y

A

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

V

V

S

-

G

-

R

-

L

-

A

A

Q

Q

E

Q

I

L

A

Q

K

R

T

E

A

T

P

P

H

N

G

-

A

S

I

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

V
x
A

A

G

N

N

R
x
P

Q
x
L

A

A

H

H

I
x
Y

D

D

T

G

T

T

G

A

P

A

E

E

I

I

W

L

D

W

Q

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

V

V

S

V

A

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

F

I

A

S

G

G

V

I

G

G

M
x
R

A

K

L

I

K

K

A

E

R

Q

N

V

K

P

D

S

V

C

K

Q

I

I

A

V

L

G

A

V

D

D

P

P

L

Y

G

G

A

S

A

I

L

L

Y

A

S

R

Y

P

Y

A

T

E

T

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

I

V

T

-

E

E

G
|
G

I
|
I

G

G

Q

Y

G

D

R

F

I

P

T

P

A

T

N

V

L

F

E

D

D

D

A

T

P

V

V

V

D

D

H

V

A

W

F

T

Q

K

I

I

T

G

D

D

E

S

E

D

A

C

V

F

P

P

I

M

V

S

F

R

D

R

L

L

L

N

E

A

H

E

E

E

G

G

L

L

C

L

L

C

G

G

S
|
S

S

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

I

L

R

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

Y

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

V

N

S

P

D

D

N

F

W

L

M

R

E

S

A

K

R

N

N

L

F

P

K

V

E

P

P

active site: K82 (= K44), S312 (= S279)
binding protoporphyrin ix containing fe: A189 (≠ V155), P192 (≠ R158), L193 (≠ Q159), Y196 (≠ I162), R229 (≠ M195)
binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K44), T109 (= T71), S110 (≠ A72), N112 (= N74), T113 (= T75), Q185 (= Q151), A218 (≠ V184), G219 (= G185), T220 (= T186), A221 (≠ G187), T223 (= T189), G268 (= G235), I269 (= I236), S312 (= S279), P338 (≠ C305), D339 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 14, 15, 16, 17, 18, 26, 27, 28

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
37% identity, 94% coverage: 7:330/343 of query aligns to 39:358/504 of Q2V0C9

query
sites
Q2V0C9

L

I

V

L

E

T

S

A

I

I

G

G

N

Q

T

T

P

P

L

L

I

I

K

K

L

L

K

N

A

I

S

P

E

K

L

S

T

Y

G

G

-

I

-

K

C

C

T

E

I

I

L

Y

G

A

K

K

A

C

E

E

F

F

M

L

N

N

P

P

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

A

L

Y

G

R

I

M

I

I

R

Q

D

D

A

A

I

E

A

D

K

K

K

G

Q

L

I

L

E

K

P

P

G

G

G

C

V

T

I

I

V

I

E

E

G

P

T

T

A

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

L

M

V

A

A

A

P

V

F

R

G

G

F

Y

K

K

T

C

V

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

S

S

Q

D

E

E

K

K

K

I

D

S

M

T

L

L

R

Y

L

A

A

L

G

G

A

A

T

K

L

I

V

I

E

R

V

T

P

P

A

T

V

E

A

A

-

S

Y

W

A

H

N

S

P

P

N

E

N

A

Y

H

V

I

K

S

V

V

S

A

G

Q

R

K

L

L

A

Q

Q

K

E

E

I

I

A

P

K

-

T

-

A

-

P

-

H

-

G

N

A

S

I

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

V

P

A

G

N

N

R

P

Q

L

A

A

H

H

I

Y

D

D

T

Q

T

T

G

A

P

I

E

E

I

I

W

W

D

K

Q

Q

T

C

D

E

G

G

K

K

V

I

D

D

G

Y

F

L

V

V

S

A

A

G

V

A

G
|
G

T
|
T

G
|
G

T
|
T

F

I

A

S

G

G

V

I

G

G

M

R

A

K

L

L

K

K

A

E

R

L

N

S

K

P

D

N

V

I

K

K

I

I

A

I

L

A

A

V

D

D

P

P

L

K

G

G

A

S

A

I

L

L

Y

D

S

P

Y

-

T

S

G

D

E

S

L

Q

K

N

A

E

E

V

G

G

S

F

S

Y

I

E

T

V

E

E

G

G

I

I

G

G

Q

Y

G

D

R

F

I

I

T

P

A

T

N

V

L

L

E

D

D

R

A

N

P

V

V

I

D

D

H

K

A

W

F

I

Q

K

I

T

T

E

D

D

E

N

E

E

A

S

V

L

P

N

I

A

V

A

F

R

D

M

L

L

L

I

E

R

H

Q

E

E

G

G

L

L

C

L

L

C

G

G

S
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S

S

S

G

G

I

A

N

A

I

L

A

I

G

A

A

A

I

L

R

K

L

I

A

A

K

K

E

D

L

I

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P

E

G

E

H

K

T

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M

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V

T

I

I

I

L

L

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D

D

Y

G

G

I

T

R

R

N

Y

Y

Q

L

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T

K

K

L

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F

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N

S

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D

Y

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P

A

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K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
N108 (= N74) binding pyridoxal 5'-phosphate
GTGGT 215:219 (= GTGGT 185:189) binding pyridoxal 5'-phosphate
S307 (= S279) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

12 binding axial binding residue
23 binding axial binding residue

5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
37% identity, 94% coverage: 7:330/343 of query aligns to 35:351/488 of 5ohxA

query
sites
5ohxA

L

I

V

L

E

T

S

A

I

I

G

G

N

Q

T

T

P

P

L

L

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I

K

K

L

L

K

N

A

I

S

P

E

K

L

S

T

Y

G

G

-

I

-

K

C

C

T

E

I

I

L

Y

G

A

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K

A

C

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E

F

F

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L

N

N

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P

G

G

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G

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S

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K
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K

D

D

R

R

A

I

A

A

L

Y

G

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M

I

I

R

Q

D

D

A

A

I

E

A

D

K

K

K

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Q

L

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K

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P

G

G

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C

V

T

I

I

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I

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E

G

P

T

T

A

S

G

G

N
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N

T

T

G

G

I

I

G

G

L

L

A

A

L

M

V

A

A

A

P

V

F

R

G

G

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Y

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T

C

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I

I

I

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V

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P

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D

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L

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L

A

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G

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L

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I

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P

A

T

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E

A

A

-

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Y

W

A

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P

N

E

N

A

Y

H

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S

A

G

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L

L

A

Q

Q

K

E

E

I

I

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P

K

-

T

-

A

-

P

-

H

-

G

N

A

S

I

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

V
x
P

A

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N

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x
P

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L

A

A

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H

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x
Y

D

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T

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T

T

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A

P

I

E

E

I

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K

Q

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T

C

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E

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G

K

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I

D

D

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L

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x
G

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G

T
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T

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G

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T

F

I

A

S

G

G

V

I

G

G

M
x
R

A

K

L

L

K

K

A

E

R

L

N

S

K

P

D

N

V

I

K

K

I

I

A

I

L

A

A

V

D

D

P

P

L

K

G

G

A

S

A

I

L

L

Y

D

S

P

Y

-

T

S

G

D

E

E

L

V

K

-

A

-

E

-

G

G

S

F

S

Y

I

E

T

V

E

E

G
|
G

I

I

G

G

Q

Y

G

D

R

F

I

I

T

P

A

T

N

V

L

L

E

D

D

R

A

N

P

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V

I

D

D

H

K

A

W

F

I

Q

K

I

T

T

E

D

D

E

N

E

E

A

S

V

L

P

N

I

A

V

A

F

R

D

M

L

L

L

I

E

R

H

Q

E

E

G

G

L

L

C

L

L

C

G

G

S
|
S

S

S

G

G

I

A

N

A

I

L

A

I

G

A

A

A

I

L

R

K

L

I

A

A

K

K

E

D

L

I

G

P

P

E

G

E

H

K

T

R

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M

V

V

T

I

I

I

L

L

C
x
P

D
|
D

Y

G

G

I

T

R

R

N

Y

Y

Q

L

S

T

K

K

L

F

F

V

N

S

P

E

D

Y

F

W

L

M

R

E

S

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R

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G

L

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A

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binding protoporphyrin ix containing fe: P181 (≠ V155), P184 (≠ R158), Y188 (≠ I162), R221 (≠ M195)
binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (≠ A183), G211 (= G185), T212 (= T186), G213 (= G187), G214 (= G188), T215 (= T189), G256 (= G235), S300 (= S279), P326 (≠ C305), D327 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 4, 7, 8, 9, 10, 14, 16, 17, 18, 19

P47998 Cysteine synthase 1; At.OAS.5-8; Beta-substituted Ala synthase 1;1; ARAth-Bsas1;1; CSase A; AtCS-A; Cys-3A; O-acetylserine (thiol)-lyase 1; OAS-TL A; O-acetylserine sulfhydrylase; Protein ONSET OF LEAF DEATH 3; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
39% identity, 90% coverage: 7:316/343 of query aligns to 9:307/322 of P47998

query
sites
P47998

L

V

V

T

E

E

S

L

I

I

G

G

N

N

T

T

P

P

L

L

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K

Y

L

L

K

N

A

V

S

A

E

E

L

-

T

-

G

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C

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-

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A

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K

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D

A

A

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A

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L

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K

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P

G

G

-

E

G

S

V

V

I

L

V

I

E

E

G

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T
|
T

A
x
S

G

G

N
|
N

T
|
T

G

G

I

V

G

G

L

L

A

A

L

F

V

T

A

A

P

A

F

K

G

G

F

Y

K

K

T

L

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I

I

I

V

T

I

M

P

P

E

A

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Q

M

S

S

Q

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E

E

K

R

D

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I

L

L

R

L

L

A

A

F

G

G

A

V

T

E

L

L

V

V

E

-

V

-

P

-

A

-

V

-

A

-

Y

L

A

T

N

D

P

P

N

A

N

K

Y

G

V

M

K

K

V

G

S

A

G

I

R

A

L

K

A

A

Q

E

E

E

I

I

A

L

K

A

T

K

A

T

P

P

H

N

G

G

A

Y

I

M

W

L

A

-

N

Q

Q
|
Q

F

F

D

E

N

N

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A

A

N

N

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Q

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A

I

H
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H

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Y

D

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G

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P

E

E

I

I

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W

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Q

G

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D

G

G

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D

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G

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F

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S

A

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|
G

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T

G
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T

F

I

A

T

G

G

V

A

G

G

M

K

A

Y

L

L

K

K

A

E

R

Q

N

N

K

A

D

N

V

V

K

K

I

L

A

Y

L

G

A

V

D

E

P

P

L

V

G

E

A

S

A

A

L

I

Y

L

S

S

Y

G

T
x
K

T

P

G

G

E

P

L
x
H

K
|
K

A

-

E

-

G

-

S

-

I

-

T

I

E

Q

G

G

I

I

G

G

Q

A

G

G

R

F

I

I

T

P

A

S

N

V

L

L

E

N

D

V

A

D

P

L

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I

D

D

H

E

A

V

F

V

Q

Q

I

V

T

S

D

S

E

D

E

E

A

S

V

I

P

D

I

M

V

A

F

R

D

Q

L

L

L

A

E

L

H

K

E

E

G

G

L

L

C

L

L

V

G

G

G

I

S
|
S

S

S

G

G

I

A

N

A

I

A

A

A

G

A

A

A

I

I

R

K

L

L

A

A

K

Q

E

R

-

P

L

E

G

N

P

A

G

G

H

K

T

L

I

F

V

V

T

A

I

I

L

F

C

P

D

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F

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G

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R

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Y

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T

L

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F

L

K46 (= K44) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
T74 (= T71) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
S75 (≠ A72) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
N77 (= N74) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
T78 (= T75) mutation T->A,S: Reduction of cysteine synthase activity.
Q147 (= Q151) mutation Q->A,E: Strong reduction of cysteine synthase activity.
H157 (= H161) mutation H->Q,N: Slight reduction of cysteine synthase activity.
G162 (= G166) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (= GTGGT 185:189) binding pyridoxal 5'-phosphate
T182 (= T186) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T189) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ T221) mutation to A: Impaired interaction with SAT1.
H221 (≠ L225) mutation to A: Impaired interaction with SAT1.
K222 (= K226) mutation to A: Impaired interaction with SAT1.
S269 (= S279) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.

Query Sequence

>WP_012171349.1 NCBI__GCF_000010525.1:WP_012171349.1
MNFRDGLVESIGNTPLIKLKKASELTGCTILGKAEFMNPGQSVKDRAALGIIRDAIAKKQ
IEPGGVIVEGTAGNTGIGLALVAAPFGFKTVIVIPETQSQEKKDMLRLAGATLVEVPAVA
YANPNNYVKVSGRLAQEIAKTAPHGAIWANQFDNVANRQAHIDTTGPEIWDQTDGKVDGF
VSAVGTGGTFAGVGMALKARNKDVKIALADPLGAALYSYYTTGELKAEGSSITEGIGQGR
ITANLEDAPVDHAFQITDEEAVPIVFDLLEHEGLCLGGSSGINIAGAIRLAKELGPGHTI
VTILCDYGTRYQSKLFNPDFLRSKNLPVPAWLEARADVPNVLV

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory