SitesBLAST

P78 (= P20) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
G85 (= G27) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T29) 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 (≠ A49) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P54) 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 (= K59) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ W65) 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 (≠ I66) to V: in CBSD; loss of activity
E131 (= E71) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G79) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ V83) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E84) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G88) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N89) binding
L154 (= L94) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A95) 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 (≠ T105) 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 (≠ Q113) 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 (= E116) 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 (≠ A120) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ V131) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ A150) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ V170) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N172) 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 (= A175) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (= D178) 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 (≠ GSGGT 200:204) binding
T257 (≠ S201) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ A206) 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 (≠ E210) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (≠ R213) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ N216) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ I219) 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 (≠ G222) 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 (= D225) to N: in CBSD; loss of activity
A288 (≠ Y232) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ S246) 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 (= G250) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G252) 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 (≠ P265) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D266) to V: in CBSD; loss of activity
R336 (≠ F281) 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 (= L283) 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 (= G292) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S294) binding ; 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 (≠ N298) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ T314) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D321) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ N324) 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 (= K329) 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
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

P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 90% coverage: 16:341/361 of query aligns to 1:316/464 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)
39% identity, 89% coverage: 22:341/361 of query aligns to 5:314/458 of 7xoyA

query
sites
7xoyA

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binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: K42 (= K59), S70 (≠ A87), N72 (= N89), T73 (= T90), T180 (≠ S201), G182 (= G203), T183 (= T204), S267 (= S294), P293 (≠ C320)

7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
39% identity, 89% coverage: 22:341/361 of query aligns to 5:314/458 of 7xnzB

query
sites
7xnzB

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P

P

E

E

I

I

W

W

R

A

D

D

T

T

D

E

G

G

K

K

V

V

D

T

G

H

F

F

I

V

C

A

A

G

V

I

G
|
G

S
x
T

G
|
G

T
|
T

L

I

A

T

G

G

V

A

A

G

E

R

G

Y

L

L

R

K

A

E

R

V

N

S

A

G

-

R

I

V

K

R

I

I

G

V

I

G

A

A

D

D

P

P

E

E

G

G

A

-

L

-

Y

-

N

S

F

V

Y

Y

A

S

H

G

G

G

E

A

L

G

K

R

S

-

G

-

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

F

S

T

V

P

P

D

D

F

E

A

I

Y

I

Q

A

I

V

P

S

D

D

A

S

E

D

A

S

V

F

P

D

Y

M

V

T

F

R

D

R

L

L

I

A

E

R

K

E

E

E

G

A

I

M

C

L

V

V

G

G

S
|
S

T

C

G

G

I

M

N

A

I

V

A

V

G

A

A

A

V

L

R

K

L

V

A

A

R

E

D

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

N

R

R

G

Y

Y

Q

M

S

S

K

K

L

I

F

F

N

N

P

D

D

A

F

W

L

M

T

S

S

S

K

Y

G

G

L

F

binding pyridoxal-5'-phosphate: K42 (= K59), G179 (= G200), T180 (≠ S201), G181 (= G202), G182 (= G203), T183 (= T204), S267 (= S294), P293 (≠ C320), D294 (= D321)

6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
34% identity, 91% coverage: 18:345/361 of query aligns to 8:333/477 of 6xwlC

query
sites
6xwlC

V

I

L

L

P

D

S

S

V

V

L

L

E

D

A

A

I

I

G

G

N

N

T

T

P

P

L

M

I

V

R

R

L

M

K

K

A

R

V

L

S

A

E

K

A

V

T

Y

G

G

-

L

-

E

C

C

N

D

I

L

L

L

G

A

K

K

A

C

E

E

F

F

L

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

W

A

I

M

I

V

R

E

Q

K

A

A

E

E

K

R

S

E

G

G

Q

R

L

L

R

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

V

L

V

A

G

A

S

A

A

V

L

R

G

G

Y

Y

R

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

A

I

L

M

R

K

L

C

L

L

G

G

A

A

E

E

L

I

V

V

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

W

R

N

N

D

P

E

N

N

N

S

Y

H

V

M

K

G

I

V

S

A

G

A

R

K

L

L

A

Q

A

R

Q

E

L

L

A

-

E

-

T

-

E

-

P

-

N

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

V

Y

D

D

T

V

T

T

A

A

P

E

E

E

I

I

W

I

R

T

D

Q

T

C

D

D

G

G

K

D

V

I

D

D

G

M

F

V

I

V

C

I

A

G

V

A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

T

G

G

V

I

A

G

E

R

G

K

L

I

R

K

A

E

R

R

N

C

A

P

A

K

I

C

K

K

I

V

G

V

I

G

A

V

D

D

P

P

E

K

G

G

A

S

A

I

L

L

Y

A

N

V

F

P

Y

D

A

S

H

L

G

N

E

D

L

E

K

K

S

R

S

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

F

K

T

V

P

V

D

D

F

E

A

W

Y

V

Q

K

I

V

P

G

D

D

A

A

E

E

A

S

V

F

P

T

Y

T

V

A

F

R

D

A

L

I

I

I

E

R

K

N

E

E

G

G

I

L

C

F

V

V

G

G

S
|
S

T

S

G

G

I

A

N

N

I

V

A

W

G

G

A

A

V

L

R

Q

L

A

A

A

R

R

D

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

N

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

T

A

S

E

K

H

G

G

L

F

P

A

V

P

P

E

D

D

binding pyridoxal-5'-phosphate: K51 (= K59), N81 (= N89), G188 (= G200), T189 (≠ S201), G190 (= G202), T192 (= T204), G238 (= G250), S282 (= S294), P308 (≠ C320), D309 (= D321)

6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
34% identity, 91% coverage: 18:345/361 of query aligns to 8:333/468 of 6xylA

query
sites
6xylA

V

I

L

L

P

D

S

S

V

V

L

L

E

D

A

A

I

I

G

G

N

N

T

T

P

P

L

M

I

V

R

R

L

M

K

K

A

R

V

L

S

A

E

K

A

V

T

Y

G

G

-

L

-

E

C

C

N

D

I

L

L

L

G

A

K

K

A

C

E

E

F

F

L

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

W

A

I

M

I

V

R

E

Q

K

A

A

E

E

K

R

S

E

G

G

Q

R

L

L

R

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

V

L

V

A

G

A

S

A

A

V

L

R

G

G

Y

Y

R

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

A

I

L

M

R

K

L

C

L

L

G

G

A

A

E

E

L

I

V

V

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

W

R

N

N

D

P

E

N

N

N

S

Y

H

V

M

K

G

I

V

S

A

G

A

R

K

L

L

A

Q

A

R

Q

E

L

L

A

-

E

-

T

-

E

-

P

-

N

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

V

Y

D

D

T

V

T

T

A

A

P

E

E

E

I

I

W

I

R

T

D

Q

T

C

D

D

G

G

K

D

V

I

D

D

G

M

F

V

I

V

C

I

A

G

V

A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

T

G

G

V

I

A

G

E

R

G

K

L

I

R

K

A

E

R

R

N

C

A

P

A

K

I

C

K

K

I

V

G

V

I

G

A

V

D

D

P

P

E

K

G

G

A

S

A

I

L

L

Y

A

N

V

F

P

Y

D

A

S

H

L

G

N

E

D

L

E

K

K

S

R

S

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

F

K

T

V

P

V

D

D

F

E

A

W

Y

V

Q

K

I

V

P

G

D

D

A

A

E

E

A

S

V

F

P

T

Y

T

V

A

F

R

D

A

L

I

I

I

E

R

K

N

E

E

G

G

I

L

C

F

V

V

G

G

S
|
S

T

S

G

G

I

A

N

N

I

V

A

W

G

G

A

A

V

L

R

Q

L

A

A

A

R

R

D

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

N

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

T

A

S

E

K

H

G

G

L

F

P

A

V

P

P

E

D

D

binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K59), T82 (= T90), Q154 (= Q166), G188 (= G200), T189 (≠ S201), G190 (= G202), T192 (= T204), G238 (= G250), I239 (= I251), Y241 (≠ Q253), S282 (= S294), P308 (≠ C320), D309 (= D321)

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
36% identity, 91% coverage: 18:344/361 of query aligns to 35:357/504 of Q2V0C9

query
sites
Q2V0C9

V

I

L

M

P

P

S

D

V

I

L

L

E

T

A

A

I

I

G

G

N

Q

T

T

P

P

L

L

I

I

R

K

L

L

K

N

A

N

V

I

S

P

E

K

A

S

T

Y

G

G

-

I

-

K

C

C

N

E

I

I

L

Y

G

A

K

K

A

C

E

E

F

F

L

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

W

R

I

M

I

I

R

Q

Q

D

A

A

E

E

K

D

S

K

G

G

Q

L

L

L

R

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

V

M

V

A

G

A

S

A

A

V

L

R

G

G

Y

Y

R

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

A

T

L

L

R

Y

L

A

L

L

G

G

A

A

E

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

P

S

Y

W

R

H

N

S

P

P

N

E

N

A

Y

H

V

I

K

S

I

V

S

A

G

Q

R

K

L

L

A

Q

A

K

Q

E

L

I

A

-

E

-

T

-

E

-

P

P

N

N

G

S

A

I

I

I

W

-

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

V

Y

D

D

T

Q

T

T

A

A

P

I

E

E

I

I

W

W

R

K

D

Q

T

C

D

E

G

G

K

K

V

I

D

D

G

Y

F

L

I

V

C

A

A

G

V

A

G
|
G

S
x
T

G
|
G

T
|
T

L

I

A

S

G

G

V

I

A

G

E

R

G

K

L

L

R

K

A

E

R

L

N

S

A

P

A

N

I

I

K

K

I

I

G

I

I

A

A

V

D

D

P

P

E

K

G

G

A

S

A

I

L

L

Y

D

N

P

F

-

Y

-

A

S

H

S

G

D

E

S

L

Q

K

N

S

E

S

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

F

N

T

V

P

I

D

D

F

K

A

W

Y

I

Q

K

I

T

P

E

D

D

A

N

E

E

A

S

V

L

P

N

Y

A

V

A

F

R

D

M

L

L

I

I

E

R

K

Q

E

E

G

G

I

L

C

L

V

C

G

G

S
|
S

T

S

G

G

I

A

N

A

I

L

A

I

G

A

A

A

V

L

R

K

L

I

A

A

R

K

D

D

L

I

G

P

P

E

G

E

H

K

T

R

I

M

V

V

T

I

I

I

L

L

C

P

D

D

Y

G

G

I

N

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

T

E

S

T

K

R

G

G

L

F

P

L

V

Q

P

P

K78 (= K59) modified: N6-(pyridoxal phosphate)lysine
N108 (= N89) binding
GTGGT 215:219 (≠ GSGGT 200:204) binding
S307 (= S294) binding

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)
36% identity, 91% coverage: 18:344/361 of query aligns to 31:350/488 of 5ohxA

query
sites
5ohxA

V

I

L

M

P

P

S

D

V

I

L

L

E

T

A

A

I

I

G

G

N

Q

T

T

P

P

L

L

I

I

R

K

L

L

K

N

A

N

V

I

S

P

E

K

A

S

T

Y

G

G

-

I

-

K

C

C

N

E

I

I

L

Y

G

A

K

K

A

C

E

E

F

F

L

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

W

R

I

M

I

I

R

Q

Q

D

A

A

E

E

K

D

S

K

G

G

Q

L

L

L

R

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

V

M

V

A

G

A

S

A

A

V

L

R

G

G

Y

Y

R

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

A

T

L

L

R

Y

L

A

L

L

G

G

A

A

E

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

P

S

Y

W

R

H

N

S

P

P

N

E

N

A

Y

H

V

I

K

S

I

V

S

A

G

Q

R

K

L

L

A

Q

A

K

Q

E

L

I

A

-

E

-

T

-

E

-

P

P

N

N

G

S

A

I

I

I

W

-

A

L

N

D

Q

Q

F

Y

D

T

N

N

V
x
P

A

G

N

N

R
x
P

Q

L

A

A

H

H

V
x
Y

D

D

T

Q

T

T

A

A

P

I

E

E

I

I

W

W

R

K

D

Q

T

C

D

E

G

G

K

K

V

I

D

D

G

Y

F

L

I

V

C

A

A
x
G

V

A

G
|
G

S
x
T

G
|
G

T
|
T

L

I

A

S

G

G

V

I

A

G

E
x
R

G

K

L

L

R

K

A

E

R

L

N

S

A

P

A

N

I

I

K

K

I

I

G

I

I

A

A

V

D

D

P

P

E

K

G

G

A

S

A

I

L

L

Y

-

N

-

F

-

Y

-

A

-

H

D

G

P

E

S

L

S

K

D

S

E

S

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

F

N

T

V

P

I

D

D

F

K

A

W

Y

I

Q

K

I

T

P

E

D

D

A

N

E

E

A

S

V

L

P

N

Y

A

V

A

F

R

D

M

L

L

I

I

E

R

K

Q

E

E

G

G

I

L

C

L

V

C

G

G

S
|
S

T

S

G

G

I

A

N

A

I

L

A

I

G

A

A

A

V

L

R

K

L

I

A

A

R

K

D

D

L

I

G

P

P

E

G

E

H

K

T

R

I

M

V

V

T

I

I

I

L

L

C
x
P

D
|
D

Y

G

G

I

N

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

T

E

S

T

K

R

G

G

L

F

P

L

V

Q

P

P

binding protoporphyrin ix containing fe: P181 (≠ V170), P184 (≠ R173), Y188 (≠ V177), R221 (≠ E210)
binding pyridoxal-5'-phosphate: K74 (= K59), N104 (= N89), G209 (≠ A198), G211 (= G200), T212 (≠ S201), G213 (= G202), G214 (= G203), T215 (= T204), G256 (= G250), S300 (= S294), P326 (≠ C320), D327 (= D321)

Sites not aligning to the query:

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

3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
35% identity, 91% coverage: 18:344/361 of query aligns to 39:362/504 of 3pc4A

query
sites
3pc4A

V

I

L

T

P

P

S

N

V

I

L

L

E

E

A

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

K

N

A

N

V

I

S

P

E

A

A

S

T

D

G

G

-

I

-

E

C

C

N

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

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

W

R

I

M

I

V

R

Q

Q

D

A

A

E

E

K

E

S

Q

G

G

Q

L

L

L

R

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

V

M

V

A

G

C

S

A

A

V

L

K

G

G

Y

Y

R

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

A

A

L

L

R

R

L

T

L

L

G

G

A

A

E

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

R

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

I

V

S

-

G

-

R

-

L

-

A

A

A

Q

Q

Q

L

L

A

Q

E

R

T

E

E

T

P

P

N

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

V
x
Y

D

D

T

G

T

T

A

A

P

A

E

E

I

I

W

L

R

W

D

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

I

V

C

V

A

S

V
x
A

G
|
G

S
x
T

G
x
A

G

G

T
|
T

L

I

A

S

G

G

V

I

A

G

E
x
R

G

K

L

I

R

K

A

E

R

Q

N

V

A

P

A

S

I

C

K

Q

I

I

G

V

I

G

A

V

D

D

P

P

E

Y

G

G

A

S

A

I

L

L

Y

A

N

R

F

-

Y

-

A

-

H

P

G

A

E

E

L

L

K

N

S

K

S

T

G

D

S

V

S

Q

I

F

-

Y

-

E

T

V

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

F

T

T

V

P

V

D

D

F

V

A

W

Y

T

Q

K

I

I

P

G

D

D

A

S

E

D

A

C

V

F

P

P

Y

M

V

S

F

R

D

R

L

L

I

N

E

A

K

E

E

E

G

G

I

L

C

L

V

C

G

G

S
|
S

T

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

V

L

R

E

L

H

A

A

R

R

D

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

N

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

T

E

S

A

K

R

G

N

L

F

P

K

V

E

P

P

active site: K82 (= K59), S312 (= S294)
binding protoporphyrin ix containing fe: A189 (≠ V170), P192 (≠ R173), L193 (≠ Q174), Y196 (≠ V177), R229 (≠ E210), T276 (≠ A258)
binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K59), T109 (= T86), S110 (≠ A87), N112 (= N89), T113 (= T90), Q185 (= Q166), A218 (≠ V199), G219 (= G200), T220 (≠ S201), A221 (≠ G202), T223 (= T204), G268 (= G250), I269 (= I251), Y271 (≠ Q253), S312 (= S294), P338 (≠ C320), D339 (= D321)

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)
35% identity, 91% coverage: 18:344/361 of query aligns to 39:362/504 of 3pc3A

query
sites
3pc3A

V

I

L

T

P

P

S

N

V

I

L

L

E

E

A

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

K

N

A

N

V

I

S

P

E

A

A

S

T

D

G

G

-

I

-

E

C

C

N

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

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

W

R

I

M

I

V

R

Q

Q

D

A

A

E

E

K

E

S

Q

G

G

Q

L

L

L

R

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

V

M

V

A

G

C

S

A

A

V

L

K

G

G

Y

Y

R

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

A

A

L

L

R

R

L

T

L

L

G

G

A

A

E

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

R

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

I

V

S

-

G

-

R

-

L

-

A

A

A

Q

Q

Q

L

L

A

Q

E

R

T

E

E

T

P

P

N

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

V
x
Y

D

D

T

G

T

T

A

A

P

A

E

E

I

I

W

L

R

W

D

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

I

V

C

V

A

S

V
x
A

G
|
G

S
x
T

G
x
A

G

G

T
|
T

L

I

A

S

G

G

V

I

A

G

E
x
R

G

K

L

I

R

K

A

E

R

Q

N

V

A

P

A

S

I

C

K

Q

I

I

G

V

I

G

A

V

D

D

P

P

E

Y

G

G

A

S

A

I

L

L

Y

A

N

R

F

-

Y

-

A

-

H

P

G

A

E

E

L

L

K

N

S

K

S

T

G

D

S

V

S

Q

I

F

-

Y

-

E

T

V

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

F

T

T

V

P

V

D

D

F

V

A

W

Y

T

Q

K

I

I

P

G

D

D

A

S

E

D

A

C

V

F

P

P

Y

M

V

S

F

R

D

R

L

L

I

N

E

A

K

E

E

E

G

G

I

L

C

L

V

C

G

G

S
|
S

T

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

V

L

R

E

L

H

A

A

R

R

D

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

N

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

T

E

S

A

K

R

G

N

L

F

P

K

V

E

P

P

active site: K82 (= K59), S312 (= S294)
binding protoporphyrin ix containing fe: A189 (≠ V170), P192 (≠ R173), L193 (≠ Q174), Y196 (≠ V177), R229 (≠ E210)
binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K59), T109 (= T86), S110 (≠ A87), N112 (= N89), T113 (= T90), Q185 (= Q166), A218 (≠ V199), G219 (= G200), T220 (≠ S201), A221 (≠ G202), T223 (= T204), G268 (= G250), I269 (= I251), S312 (= S294), P338 (≠ C320), D339 (= D321)

Sites not aligning to the query:

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

6c4pA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex (see paper)
34% identity, 89% coverage: 21:341/361 of query aligns to 9:335/344 of 6c4pA

query
sites
6c4pA

S

N

V

V

L

I

E

D

A

L

I

V

G

G

N

N

T

T

P

P

L

L

I

I

R

A

L

L

K

K

A

K

V

L

S

P

E

K

A

A

T

L

G

G

C

I

-

K

-

P

N

Q

I

I

L

Y

G

A

K

K

A

L

E

E

F

L

L

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

W

S

I

M

I

V

R

E

Q

E

A

A

E

E

K

A

S

S

G

G

Q

R

L

I

R

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

V

L

V

I

G

G

S

A

A

I

L

K

G

G

Y

Y

R

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

A

V

L

L

R

K

L

A

L

L

G

G

A

A

E

E

L

I

V

I

E

R

V

T

P

P

-

T

A

A

V

A

P

A

Y

W

R

D

N

S

P

P

N

E

N

S

Y

H

V

I

K

G

I

V

S

A

G

K

R

K

L

L

A

-

Q

-

L

-

A

-

E

E

T

K

E

E

P

I

N

P

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

V

Y

D

F

T

G

T

T

A

G

P

R

E

E

I

I

W

Q

R

R

D

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

I

V

C

A

A

G

V
x
A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

S

G

G

V

I

A

S

E

K

G

Y

L

L

R

K

A

E

R

Q

N

N

A

D

A

K

I

I

K

Q

I

I

G

V

I

G

A

A

D

D

P

P

E

F

G

G

A

S

A

I

L

L

Y

A

N

Q

F

P

Y

E

A

N

H

L

G

N

E

K

L

T

K

D

S

I

S

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

F

K

T

L

P

I

D

D

F

V

A

W

Y

Y

Q

K

I

T

P

D

D

D

A

K

E

P

A

S

V

F

P

K

Y

Y

V

A

F

R

D

Q

L

L

I

I

E

S

K

N

E

E

G

G

I

V

C

L

V

V

G

G

S
|
S

T

S

G

G

I

S

N

A

I

F

A

T

G

A

A

V

V

V

R

K

L

Y

A

C

R

E

D

D

-

H

-

P

-

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

N

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

T

K

S

K

K

N

G

N

L

L

binding calcium ion: N179 (vs. gap), D182 (≠ G190), N183 (≠ K191)
binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: K49 (= K59), N80 (= N89), A191 (≠ V199), G192 (= G200), T193 (≠ S201), G194 (= G202), T196 (= T204), G241 (= G250), S285 (= S294), P314 (≠ C320), D315 (= D321)

6c2zA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-aminoacrylate intermediate (see paper)
34% identity, 89% coverage: 21:341/361 of query aligns to 10:336/345 of 6c2zA

query
sites
6c2zA

S

N

V

V

L

I

E

D

A

L

I

V

G

G

N

N

T

T

P

P

L

L

I

I

R

A

L

L

K

K

A

K

V

L

S

P

E

K

A

A

T

L

G

G

C

I

-

K

-

P

N

Q

I

I

L

Y

G

A

K

K

A

L

E

E

F

L

L

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

W

S

I

M

I

V

R

E

Q

E

A

A

E

E

K

A

S

S

G

G

Q

R

L

I

R

H

P

P

G

S

-

R

G

S

V

T

I

L

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

V

L

V

I

G

G

S

A

A

I

L

K

G

G

Y

Y

R

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

A

V

L

L

R

K

L

A

L

L

G

G

A

A

E

E

L

I

V

I

E

R

V

T

P

P

-

T

A

A

V

A

P

A

Y

W

R

D

N

S

P

P

N

E

N

S

Y

H

V

I

K

G

I

V

S

A

G

K

R

K

L

L

A

-

Q

-

L

-

A

-

E

E

T

K

E

E

P

I

N

P

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

V

Y

D

F

T

G

T

T

A

G

P

R

E

E

I

I

W

Q

R

R

D

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

I

V

C

A

A

G

V
x
A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

S

G

G

V

I

A

S

E

K

G

Y

L

L

R

K

A

E

R

Q

N

N

A

D

A

K

I

I

K

Q

I

I

G

V

I

G

A

A

D

D

P

P

E

F

G

G

A

S

A

I

L

L

Y

A

N

Q

F

P

Y

E

A

N

H

L

G

N

E

K

L

T

K

D

S

I

S

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

F

K

T

L

P

I

D

D

F

V

A

W

Y

Y

Q

K

I

T

P

D

D

D

A

K

E

P

A

S

V

F

P

K

Y

Y

V

A

F

R

D

Q

L

L

I

I

E

S

K

N

E

E

G

G

I

V

C

L

V

V

G

G

S
|
S

T

S

G

G

I

S

N

A

I

F

A

T

G

A

A

V

V

V

R

K

L

Y

A

C

R

E

D

D

-

H

-

P

-

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

N

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

T

K

S

K

K

N

G

N

L

L

binding calcium ion: N180 (vs. gap), D183 (≠ G190), N184 (≠ K191)
binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K50 (= K59), T78 (= T86), S79 (≠ A87), N81 (= N89), T82 (= T90), Q154 (= Q166), A192 (≠ V199), G193 (= G200), T194 (≠ S201), G195 (= G202), T197 (= T204), G242 (= G250), S286 (= S294), P315 (≠ C320), D316 (= D321)

6c2qA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the plp-l-serine intermediate (see paper)
34% identity, 89% coverage: 21:341/361 of query aligns to 10:336/345 of 6c2qA

query
sites
6c2qA

S

N

V

V

L

I

E

D

A

L

I

V

G

G

N

N

T

T

P

P

L

L

I

I

R

A

L

L

K

K

A

K

V

L

S

P

E

K

A

A

T

L

G

G

C

I

-

K

-

P

N

Q

I

I

L

Y

G

A

K

K

A

L

E

E

F

L

L

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

W

S

I

M

I

V

R

E

Q

E

A

A

E

E

K

A

S

S

G

G

Q

R

L

I

R

H

P

P

G

S

-

R

G

S

V

T

I

L

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

V

L

V

I

G

G

S

A

A

I

L

K

G

G

Y

Y

R

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

A

V

L

L

R

K

L

A

L

L

G

G

A

A

E

E

L

I

V

I

E

R

V

T

P

P

-

T

A

A

V

A

P

A

Y

W

R

D

N

S

P

P

N

E

N

S

Y

H

V

I

K

G

I

V

S

A

G

K

R

K

L

L

A

-

Q

-

L

-

A

-

E

E

T

K

E

E

P

I

N

P

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

V

Y

D

F

T

G

T

T

A

G

P

R

E

E

I

I

W

Q

R

R

D

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

I

V

C

A

A

G

V
x
A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

S

G

G

V

I

A

S

E

K

G

Y

L

L

R

K

A

E

R

Q

N

N

A

D

A

K

I

I

K

Q

I

I

G

V

I

G

A

A

D

D

P

P

E

F

G

G

A

S

A

I

L

L

Y

A

N

Q

F

P

Y

E

A

N

H

L

G

N

E

K

L

T

K

D

S

I

S

T

G

D

S

Y

S

K

I

V

T

-

E

E

G
|
G

I

I

G

G

Q
x
Y

G

D

R

F

I

V

T

P

A

Q

N

V

L

L

E

D

D

R

F

K

T

L

P

I

D

D

F

V

A

W

Y

Y

Q

K

I

T

P

D

D

D

A

K

E

P

A

S

V

F

P

K

Y

Y

V

A

F

R

D

Q

L

L

I

I

E

S

K

N

E

E

G

G

I

V

C

L

V

V

G

G

S
|
S

T

S

G

G

I

S

N

A

I

F

A

T

G

A

A

V

V

V

R

K

L

Y

A

C

R

E

D

D

-

H

-

P

-

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

N

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

T

K

S

K

K

N

G

N

L

L

binding calcium ion: N180 (vs. gap), D183 (≠ G190), N184 (≠ K191)
binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: K50 (= K59), T78 (= T86), S79 (≠ A87), N81 (= N89), T82 (= T90), Q154 (= Q166), A192 (≠ V199), G193 (= G200), T194 (≠ S201), G195 (= G202), T197 (= T204), G242 (= G250), Y245 (≠ Q253), S286 (= S294), P315 (≠ C320), D316 (= D321)

6c2hA Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the catalytic core (see paper)
34% identity, 89% coverage: 21:341/361 of query aligns to 10:336/345 of 6c2hA

query
sites
6c2hA

S

N

V

V

L

I

E

D

A

L

I

V

G

G

N

N

T

T

P

P

L

L

I

I

R

A

L

L

K

K

A

K

V

L

S

P

E

K

A

A

T

L

G

G

C

I

-

K

-

P

N

Q

I

I

L

Y

G

A

K

K

A

L

E

E

F

L

L

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

W

S

I

M

I

V

R

E

Q

E

A

A

E

E

K

A

S

S

G

G

Q

R

L

I

R

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

V

L

V

I

G

G

S

A

A

I

L

K

G

G

Y

Y

R

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

A

V

L

L

R

K

L

A

L

L

G

G

A

A

E

E

L

I

V

I

E

R

V

T

P

P

-

T

A

A

V

A

P

A

Y

W

R

D

N

S

P

P

N

E

N

S

Y

H

V

I

K

G

I

V

S

A

G

K

R

K

L

L

A

-

Q

-

L

-

A

-

E

E

T

K

E

E

P

I

N

P

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

V

Y

D

F

T

G

T

T

A

G

P

R

E

E

I

I

W

Q

R

R

D

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

I

V

C

A

A

G

V
x
A

G
|
G

S
x
T

G
|
G

G

G

T
|
T

L

I

A

S

G

G

V

I

A

S

E

K

G

Y

L

L

R

K

A

E

R

Q

N

N

A

D

A

K

I

I

K

Q

I

I

G

V

I

G

A

A

D

D

P

P

E

F

G

G

A

S

A

I

L

L

Y

A

N

Q

F

P

Y

E

A

N

H

L

G

N

E

K

L

T

K

D

S

I

S

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

F

K

T

L

P

I

D

D

F

V

A

W

Y

Y

Q

K

I

T

P

D

D

D

A

K

E

P

A

S

V

F

P

K

Y

Y

V

A

F

R

D

Q

L

L

I

I

E

S

K

N

E

E

G

G

I

V

C

L

V

V

G

G

S
|
S

T

S

G

G

I

S

N

A

I

F

A

T

G

A

A

V

V

V

R

K

L

Y

A

C

R

E

D

D

-

H

-

P

-

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

N

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

T

K

S

K

K

N

G

N

L

L

binding calcium ion: N180 (vs. gap), D183 (≠ G190), N184 (≠ K191)
binding pyridoxal-5'-phosphate: K50 (= K59), N81 (= N89), A192 (≠ V199), G193 (= G200), T194 (≠ S201), G195 (= G202), T197 (= T204), G242 (= G250), S286 (= S294), P315 (≠ C320), D316 (= D321)

3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
35% identity, 91% coverage: 18:344/361 of query aligns to 37:360/500 of 3pc2A

query
sites
3pc2A

V

I

L

T

P

P

S

N

V

I

L

L

E

E

A

V

I

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

K

N

A

N

V

I

S

P

E

A

A

S

T

D

G

G

-

I

-

E

C

C

N

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

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

W

R

I

M

I

V

R

Q

Q

D

A

A

E

E

K

E

S

Q

G

G

Q

L

L

L

R

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

V

M

V

A

G

C

S

A

A

V

L

K

G

G

Y

Y

R

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

A

A

L

L

R

R

L

T

L

L

G

G

A

A

E

K

L

I

V

I

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

R

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

I

V

S

-

G

-

R

-

L

-

A

A

A

Q

Q

Q

L

L

A

Q

E

R

T

E

E

T

P

P

N

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

V
x
Y

D

D

T

G

T

T

A

A

P

A

E

E

I

I

W

L

R

W

D

Q

T

L

D

D

G

N

K

K

V

V

D

D

G

M

F

I

I

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C

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A

S

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x
A

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|
G

S
x
T

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x
A

G

G

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T

L

I

A

S

G

G

V

I

A

G

E
x
R

G

K

L

I

R

K

A

E

R

Q

N

V

A

P

A

S

I

C

K

Q

I

I

G

V

I

G

A

V

D

D

P

P

E

Y

G

G

A

S

A

I

L

L

Y

A

N

R

F

-

Y

-

A

-

H

P

G

A

E

E

L

L

K

N

S

K

S

T

G

D

S

V

S

Q

I

F

-

Y

-

E

T

V

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

F

T

T

V

P

V

D

D

F

V

A

W

Y

T

Q

K

I

I

P

G

D

D

A

S

E

D

A

C

V

F

P

P

Y

M

V

S

F

R

D

R

L

L

I

N

E

A

K

E

E

E

G

G

I

L

C

L

V

C

G

G

S
|
S

T

S

G

G

I

G

N

A

I

M

A

H

G

A

A

A

V

L

R

E

L

H

A

A

R

R

D

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

N

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

T

E

S

A

K

R

G

N

L

F

P

K

V

E

P

P

active site: K80 (= K59), S310 (= S294)
binding protoporphyrin ix containing fe: A187 (≠ V170), P190 (≠ R173), L191 (≠ Q174), Y194 (≠ V177), R227 (≠ E210)
binding pyridoxal-5'-phosphate: K80 (= K59), N110 (= N89), A216 (≠ V199), G217 (= G200), T218 (≠ S201), A219 (≠ G202), T221 (= T204), G266 (= G250), S310 (= S294), P336 (≠ C320), D337 (= D321)

Sites not aligning to the query:

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

6vjuB Crystal structure of cystathionine beta synthase from legionella pneumophila with llp, plp, and homocysteine
35% identity, 90% coverage: 18:341/361 of query aligns to 3:316/317 of 6vjuB

query
sites
6vjuB

V

I

L

Y

P

P

S

N

V

I

L

L

E

A

A

T

I

I

G

G

N

H

T

T

P

P

L

V

I

V

R

K

L

I

K

N

A

R

V

L

S

G

E

K

A

D

T

L

G

E

C

C

N

E

I

L

L

Y

G

A

K

K

A

C

E

E

F

F

L

F

N

N

P

P

G

G

Q

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

W

E

I

M

I

V

R

V

Q

K

A

A

E

E

K

K

S

E

G

G

Q

R

L

I

R

K

P

P

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

I

A

A

V

L

V

A

G

G

S

A

A

V

L

L

G

G

Y

Y

R

K

T

V

V

I

I

I

V

T

I

M

P

P

E

E

T

K

Q

M

S

S

Q

Q

E

E

K

K

K

Q

D

S

A

V

L

L

R

E

L

R

L

L

G

G

A

A

E

I

L

I

V

Y

E

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

R

N

N

D

P

P

N

D

N

S

Y

H

V

I

K

S

I

L

S

A

G

K

R

K

L

L

A

Q

A

A

Q

E

L

I

A

-

E

-

T

-

E

-

P

P

N

N

G

S

A

H

I

I

W

L

A

-

N

D

Q

Q

F

Y

D

A

N

N

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A

N

N

N

R

P

Q

N

A

A

H

H

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Y

D

F

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A

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Q

E

E

I

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D

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T

F

D

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G

K

K

D

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D

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F

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C

A

A

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|
G

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x
T

G
|
G

G

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T
|
T

L

I

A

T

G

G

V

I

A

A

E

K

G

R

L

L

R

K

A

E

R

F

N

N

A

P

A

A

I

I

K

K

I

I

G

I

I

G

A

A

D

D

P

P

E

E

G

G

A

S

A

I

L

L

Y

-

N

-

F

-

Y

-

A

-

H

-

G

G

E

G

L

G

K

T

S

E

S

I

G

K

S

S

S

Y

I

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E

E

G
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G

I

I

G

G

Q

Y

G

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F

I

F

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A

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N

V

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L

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D

N

F

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T

L

P

I

D

D

F

A

A

Y

Y

I

Q

K

I

T

P

N

D

D

A

A

E

D

A

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F

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R

Y

T

V

A

F

R

D

R

L

L

I

I

E

K

K

E

E

E

G

G

I

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C

L

V

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S

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C

G

G

I

A

N

A

I

M

A

W

G

A

A

A

V

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Q

L

A

A

A

R

K

D

S

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L

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S

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K

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K

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V

I

I

L

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C
x
P

D
|
D

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G

I

N

R

R

N

Y

Y

Q

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S

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K

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F

binding pyridoxal-5'-phosphate: K44 (= K59), N74 (= N89), G181 (= G200), T182 (≠ S201), G183 (= G202), T185 (= T204), G225 (= G250), S269 (= S294), P295 (≠ C320), D296 (= D321)

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
38% identity, 84% coverage: 25:328/361 of query aligns to 6:297/302 of 2efyA

query
sites
2efyA

A

A

I

I

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G

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K

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T

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R

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L

K

A

A

K

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E

A

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T

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M

C

A

N

E

I

V

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V

K

K

A

L

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E

F

G

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L

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N

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P

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G

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K

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D

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R

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P

A

A

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W

Y

I

M

I

I

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Q

D

A

A

E

E

K

E

S

R

G

G

Q

I

L

L

R

R

P

P

G

G

G

S

-

G

-

Q

V

V

I

I

V

V

E

E

G

P

T
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T

A
x
S

G
|
G

N
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N

T
|
T

G

G

I

I

G

G

L

L

A

A

V

M

V

I

G

A

S

A

A

S

L

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G

Y

Y

R

R

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I

I

L

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T

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M

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P

E

A

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Q

M

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Q

E

E

E

K

R

K

K

D

R

A

V

L

L

R

K

L

A

L

F

G

G

A

A

E

E

L

L

V

V

E

-

V

-

P

-

A

-

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-

Y

L

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T

N

D

P

P

N

E

N

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Y

R

V

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K

L

I

A

S

A

G

R

R

E

L

E

A

A

A

L

Q

R

L

L

A

K

E

E

T

E

E

-

P

-

N

L

G

G

A

A

I

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

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P

A

A

N

N

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Q

R

A

A

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H

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Y

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P

E

E

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A

T

L

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E

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F

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x
Y

A

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G
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G

S
x
T

G
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G

G

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|
T

L

I

A

T

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G

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V

A

G

E

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G

Y

L

L

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A

E

R

R

N

I

A

P

A

H

I

V

K

K

I

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I

I

A

A

V

D
x
E

P

P

E

-

G

-

A

-

A

A

L

R

Y
x
S

N

N

F

V

Y

L

A

S

H

G

G

G

E

K

L

M

K

G

S

Q

S

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

F

S

T

L

P

L

D

D

F

G

A

V

Y

I

Q

Q

I

V

P

W

D

E

A

E

E

D

A

A

V

F

P

P

Y

L

V

A

F

R

D

R

L

L

I

A

E

R

K

E

E

E

G

G

I

L

C

F

V

L

G

G

G

M

S
|
S

T

S

G

G

I

G

N

I

I

V

A

W

G

A

A

A

V

L

R

Q

L

V

A

A

R

R

D

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

N

W

R

K

Y

Y

Q

L

S

S

active site: K40 (= K59), S70 (≠ A87), E200 (≠ D225), S204 (≠ Y232), S263 (= S294)
binding 5-oxohexanoic acid: T69 (= T86), G71 (= G88), T73 (= T90), Q141 (= Q166), G175 (= G200), G219 (= G250), M220 (≠ I251), P222 (≠ Q253)
binding pyridoxal-5'-phosphate: K40 (= K59), N72 (= N89), Y172 (≠ C197), G175 (= G200), T176 (≠ S201), G177 (= G202), T179 (= T204), G219 (= G250), S263 (= S294), P289 (≠ C320), D290 (= D321)

Query Sequence

>SMc01174 FitnessBrowser__Smeli:SMc01174
MANAGIRSVQREVFNMPVLPSVLEAIGNTPLIRLKAVSEATGCNILGKAEFLNPGQSVKD
RAALWIIRQAEKSGQLRPGGVIVEGTAGNTGIGLAVVGSALGYRTVIVIPETQSQEKKDA
LRLLGAELVEVPAVPYRNPNNYVKISGRLAAQLAETEPNGAIWANQFDNVANRQAHVDTT
APEIWRDTDGKVDGFICAVGSGGTLAGVAEGLRARNAAIKIGIADPEGAALYNFYAHGEL
KSSGSSITEGIGQGRITANLEDFTPDFAYQIPDAEAVPYVFDLIEKEGICVGGSTGINIA
GAVRLARDLGPGHTIVTILCDYGNRYQSKLFNPDFLTSKGLPVPDWLKTASNIAVPYEPA
G

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