SitesBLAST

P78 (= P5) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
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 (≠ Y50) 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 (= E56) 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 (= C90) 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 (≠ A105) 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 (≠ L150) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N152) 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 (= A155) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ E158) 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 180:184) binding pyridoxal 5'-phosphate
T257 (= T181) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ A186) 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 (≠ L190) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K193) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ N196) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ I199) 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 (≠ V202) 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 (= D205) to N: in CBSD; loss of activity
A288 (≠ Y212) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ S226) 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 (= G230) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G232) 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 (≠ I245) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D246) to V: in CBSD; loss of activity
R336 (≠ Y261) 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 (= L263) 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 (= G272) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S274) 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 (≠ N278) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ T294) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D301) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ T304) 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 (= K309) 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

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 99% coverage: 3:325/326 of query aligns to 36:360/500 of 7qgtB

query
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7qgtB

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binding protoporphyrin ix containing fe: A186 (≠ L150), P189 (≠ R153), L190 (≠ I154), Y193 (= Y157), R226 (≠ L190)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (≠ A72), N109 (= N74), T110 (= T75), Q182 (= Q146), G216 (= G180), T217 (= T181), G218 (= G182), T220 (= T184), G265 (= G230), S309 (= S274), P335 (≠ C300), D336 (= D301)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 10, 11, 12, 13, 14, 23, 24, 25

1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
40% identity, 98% coverage: 3:322/326 of query aligns to 34:348/348 of 1jbqA

query
sites
1jbqA

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active site: K77 (= K44), S105 (≠ A72), D232 (= D205), S236 (= S209), L238 (= L211), S300 (= S274), P326 (≠ C300)
binding protoporphyrin ix containing fe: A177 (≠ L150), P180 (≠ R153), L181 (≠ I154), Y184 (= Y157), R217 (≠ L190)
binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), V206 (≠ T179), G207 (= G180), T208 (= T181), G209 (= G182), G210 (= G183), T211 (= T184), G256 (= G230), S300 (= S274), P326 (≠ C300), D327 (= D301)

Sites not aligning to the query:

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

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
42% identity, 98% coverage: 3:322/326 of query aligns to 35:355/504 of Q2V0C9

query
sites
Q2V0C9

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Q

M

S

S

V

D

E

E

K

K

M

I

D

S

A

T

L

L

R

Y

T

A

L

L

G

G

A

A

E

K

V

I

K

I

P

R

V

T

P

P

A

T

-

E

V

A

P

S

Y

W

K

H

N

S

P

P

N

E

N

A

Y

H

V

I

K

S

M

V

S

A

G

Q

K

K

L

L

A

Q

S

K

T

E

I

I

E

P

N

N

A

S

I

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

L

P

A

G

N

N

R

P

I

L

A

A

H

H

Y

Y

E

D

T

Q

T

T

G

A

P

I

E

E

I

I

W

W

E

K

Q

Q

T

C

D

E

G

G

K

K

V

I

D

D

A

Y

W

L

V

V

A

A

A

G

T

A

G
|
G

T
|
T

G
|
G

T
|
T

F

I

A

S

G

G

V

I

S

G

L

R

F

K

L

L

K

K

E

E

K

L

N

S

P

P

Q

N

I

I

K

K

T

I

V

I

L

A

A

V

D

D

P

P

M

K

G

G

S

S

G

I

L

L

Y

D

S

P

Y

-

V

-

K

S

T

S

G

D

E

S

I

Q

S

N

S

E

E

V

G

G

N

F

S

Y

I

E

T

V

E

E

G

G

I

I

G

G

N

Y

S

D

R

F

I

I

T

P

K

T

N

V

M

L

E

D

N

R

V

N

M

V

I

I

D

D

D

K

A

W

I

I

R

K

V

T

D

E

D

D

K

N

E

E

A

S

V

L

R

N

V

A

Y

R

Q

M

L

L

L

I

R

R

K

Q

D

E

G

G

L

L

F

L

M

C

G

G

S
|
S

V

S

G

G

I

A

N

A

V

L

G

I

A

A

V

L

A

K

L

I

A

A

K

K

Q

D

M

I

G

P

P

E

G

E

H

K

T

R

I

M

V

V

T

I

V

I

L

L

C

P

D

D

S

G

G

I

T

R

R

N

Y

Y

Q

L

S

T

K

K

L

F

F

V

N

S

R

E

E

Y

W

W

L

M

A

E

T

T

K

R

N

G

L

F

L

L

K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
N108 (= N74) binding pyridoxal 5'-phosphate
GTGGT 215:219 (= GTGGT 180:184) binding pyridoxal 5'-phosphate
S307 (= S274) 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)
42% identity, 98% coverage: 3:322/326 of query aligns to 31:348/488 of 5ohxA

query
sites
5ohxA

I

I

K

M

P

P

G

D

F

I

I

L

G

T

T

A

V

I

G

G

N

Q

T

T

P

P

L

L

I

I

R

K

L

L

N

N

S

N

F

I

S

P

E

K

E

S

T

Y

G

G

-

I

-

K

C

C

E

E

I

I

L

Y

G

A

K

K

A

C

E

E

F

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

A

L

Y

Y

R

I

M

I

I

K

Q

D

D

A

A

E

E

E

D

K

K

G

G

L

L

K

K

P

P

G

G

G

C

T

T

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

H

M

I

A

C

A

N

A

A

V

K

R

G

G

Y

Y

K

K

C

C

L

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

S

S

V

D

E

E

K

K

M

I

D

S

A

T

L

L

R

Y

T

A

L

L

G

G

A

A

E

K

V

I

K

I

P

R

V

T

P

P

A

T

-

E

V

A

P

S

Y

W

K

H

N

S

P

P

N

E

N

A

Y

H

V

I

K

S

M

V

S

A

G

Q

K

K

L

L

A

Q

S

K

T

E

I

I

E

P

N

N

A

S

I

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

L
x
P

A

G

N

N

R
x
P

I

L

A

A

H

H

Y
|
Y

E

D

T

Q

T

T

G

A

P

I

E

E

I

I

W

W

E

K

Q

Q

T

C

D

E

G

G

K

K

V

I

D

D

A

Y

W

L

V

V

A

A

A
x
G

T

A

G
|
G

T
|
T

G
|
G

T
|
T

F

I

A

S

G

G

V

I

S

G

L
x
R

F

K

L

L

K

K

E

E

K

L

N

S

P

P

Q

N

I

I

K

K

T

I

V

I

L

A

A

V

D

D

P

P

M

K

G

G

S

S

G

I

L

L

Y

-

S

-

Y

-

V

-

K

-

T

-

G

-

E

D

I

P

S

S

E

D

-

E

-

V

G

G

N

F

S

Y

I

E

T

V

E

E

G
|
G

I

I

G

G

N

Y

S

D

R

F

I

I

T

P

K

T

N

V

M

L

E

D

N

R

V

N

M

V

I

I

D

D

D

K

A

W

I

I

R

K

V

T

D

E

D

D

K

N

E

E

A

S

V

L

R

N

V

A

Y

R

Q

M

L

L

L

I

R

R

K

Q

D

E

G

G

L

L

F

L

M

C

G

G

S
|
S

V

S

G

G

I

A

N

A

V

L

G

I

A

A

V

L

A

K

L

I

A

A

K

K

Q

D

M

I

G

P

P

E

G

E

H

K

T

R

I

M

V

V

T

I

V

I

L

L

C
x
P

D
|
D

S

G

G

I

T

R

R

N

Y

Y

Q

L

S

T

K

K

L

F

F

V

N

S

R

E

E

Y

W

W

L

M

A

E

T

T

K

R

N

G

L

F

L

L

binding protoporphyrin ix containing fe: P181 (≠ L150), P184 (≠ R153), Y188 (= Y157), R221 (≠ L190)
binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (≠ A178), G211 (= G180), T212 (= T181), G213 (= G182), G214 (= G183), T215 (= T184), G256 (= G230), S300 (= S274), P326 (≠ C300), D327 (= D301)

Sites not aligning to the query:

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

3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
39% identity, 98% coverage: 3:321/326 of query aligns to 37:357/500 of 3pc2A

query
sites
3pc2A

I

I

K

T

P

P

G

N

F

I

I

L

G

E

T

V

V

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

N

N

S

N

F

I

S

P

E

A

E

S

T

D

G

G

-

I

-

E

C

C

E

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

Y

R

I

M

I

V

K

Q

D

D

A

A

E

E

K

Q

G

G

L

L

K

K

P

P

G

G

G

Y

T

T

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

H

M

I

A

C

C

N

A

A

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K

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G

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Y

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C

L

I

I

I

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V

I

M

P

P

E

E

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K

Q

M

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S

V

N

E

E

K

K

M

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D

S

A

A

L

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T

L

L

G

G

A

A

E

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I

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R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

K

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

M

V

S

A

G

Q

K

Q

L

L

A

Q

S

R

T

E

I

T

E

P

N

N

A

S

I

I

W

V

A

L

N

D

Q

Q

F

Y

D

R

N

N

L
x
A

A

G

N

N

R
x
P

I
x
L

A

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Y
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Y

E

D

T

G

T

T

G

A

P

A

E

E

I

I

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L

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W

Q

Q

T

L

D

D

G

N

K

K

V

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M

W

I

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V

A

V

A

S

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x
A

G
|
G

T
|
T

G
x
A

G

G

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|
T

F

I

A

S

G

G

V

I

S

G

L
x
R

F

K

L

I

K

K

E

E

K

Q

N

V

P

P

Q

S

I

C

K

Q

T

I

V

V

L

G

A

V

D

D

P

P

M

Y

G

G

S

S

G

I

L

L

Y

A

S

R

Y

P

V

A

K

E

T

L

G

N

E

K

I

T

S

D

S

V

E

Q

G

F

N

Y

S

E

I

V

T

-

E

E

G
|
G

I

I

G

G

N

Y

S

D

R

F

I

P

T

P

K

T

N

V

M

F

E

D

N

D

V

T

M

V

I

V

D

D

D

V

A

W

I

T

R

K

V

I

D

G

D

D

K

S

E

D

A

C

V

F

R

P

V

M

V

S

Y

R

Q

R

L

L

L

N

R

A

K

E

D

E

G

G

L

L

F

L

M

C

G

G

S
|
S

V

S

G

G

I

G

N

A

V

M

G

H

A

A

V

L

A

E

L

H

A

A

K

R

Q

K

M

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

V

I

L

L

C
x
P

D
|
D

S

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

V

N

S

R

D

E

N

W

W

L

M

A

E

T

A

K

R

N

N

L

F

active site: K80 (= K44), S310 (= S274)
binding protoporphyrin ix containing fe: A187 (≠ L150), P190 (≠ R153), L191 (≠ I154), Y194 (= Y157), R227 (≠ L190)
binding pyridoxal-5'-phosphate: K80 (= K44), N110 (= N74), A216 (≠ T179), G217 (= G180), T218 (= T181), A219 (≠ G182), T221 (= T184), G266 (= G230), S310 (= S274), P336 (≠ C300), D337 (= D301)

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)
39% identity, 98% coverage: 3:321/326 of query aligns to 39:359/504 of 3pc4A

query
sites
3pc4A

I

I

K

T

P

P

G

N

F

I

I

L

G

E

T

V

V

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

N

N

S

N

F

I

S

P

E

A

E

S

T

D

G

G

-

I

-

E

C

C

E

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

Y

R

I

M

I

V

K

Q

D

D

A

A

E

E

K

Q

G

G

L

L

K

K

P

P

G

G

G

Y

T

T

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

H

M

I

A

C

C

N

A

A

V

K

K

G

G

Y

Y

K

K

C

C

L

I

I

I

V

V

I

M

P

P

E

E

T

K

Q

M

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S

V

N

E

E

K

K

M

V

D

S

A

A

L

L

R

R

T

T

L

L

G

G

A

A

E

K

V

I

K

I

P

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

K

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

M

V

S

A

G

Q

K

Q

L

L

A

Q

S

R

T

E

I

T

E

P

N

N

A

S

I

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

L
x
A

A

G

N

N

R
x
P

I
x
L

A

A

H

H

Y
|
Y

E

D

T

G

T

T

G

A

P

A

E

E

I

I

W

L

E

W

Q

Q

T

L

D

D

G

N

K

K

V

V

D

D

A

M

W

I

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V

A

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x
A

G
|
G

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|
T

G
x
A

G

G

T
|
T

F

I

A

S

G

G

V

I

S

G

L
x
R

F

K

L

I

K

K

E

E

K

Q

N

V

P

P

Q

S

I

C

K

Q

T

I

V

V

L

G

A

V

D

D

P

P

M

Y

G

G

S

S

G

I

L

L

Y

A

S

R

Y

P

V

A

K

E

T

L

G

N

E

K

I

T

S

D

S

V

E

Q

G

F

N

Y

S

E

I

V

T

-

E

E

G
|
G

I
|
I

G

G

N
x
Y

S

D

R

F

I

P

T

P

K
x
T

N

V

M

F

E

D

N

D

V

T

M

V

I

V

D

D

D

V

A

W

I

T

R

K

V

I

D

G

D

D

K

S

E

D

A

C

V

F

R

P

V

M

V

S

Y

R

Q

R

L

L

L

N

R

A

K

E

D

E

G

G

L

L

F

L

M

C

G

G

S
|
S

V

S

G

G

I

G

N

A

V

M

G

H

A

A

V

L

A

E

L

H

A

A

K

R

Q

K

M

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

V

I

L

L

C
x
P

D
|
D

S

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

V

N

S

R

D

E

N

W

W

L

M

A

E

T

A

K

R

N

N

L

F

active site: K82 (= K44), S312 (= S274)
binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ R153), L193 (≠ I154), Y196 (= Y157), R229 (≠ L190), T276 (≠ K238)
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 (= Q146), A218 (≠ T179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G230), I269 (= I231), Y271 (≠ N233), S312 (= S274), P338 (≠ C300), D339 (= D301)

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)
39% identity, 98% coverage: 3:321/326 of query aligns to 39:359/504 of 3pc3A

query
sites
3pc3A

I

I

K

T

P

P

G

N

F

I

I

L

G

E

T

V

V

I

G

G

N

C

T

T

P

P

L

L

I

V

R

K

L

L

N

N

S

N

F

I

S

P

E

A

E

S

T

D

G

G

-

I

-

E

C

C

E

E

I

M

L

Y

G

A

K

K

A

C

E

E

F

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

Y

R

I

M

I

V

K

Q

D

D

A

A

E

E

K

Q

G

G

L

L

K

K

P

P

G

G

G

Y

T

T

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

H

M

I

A

C

C

N

A

A

V

K

K

G

G

Y

Y

K

K

C

C

L

I

I

I

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V

I

M

P

P

E

E

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K

Q

M

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S

V

N

E

E

K

K

M

V

D

S

A

A

L

L

R

R

T

T

L

L

G

G

A

A

E

K

V

I

K

I

P

R

V

T

P

P

A

T

-

E

V

A

P

A

Y

Y

K

D

N

S

P

P

N

E

N

G

Y

L

V

I

K

Y

M

V

S

A

G

Q

K

Q

L

L

A

Q

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R

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E

I

T

E

P

N

N

A

S

I

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

L
x
A

A

G

N

N

R
x
P

I
x
L

A

A

H

H

Y
|
Y

E

D

T

G

T

T

G

A

P

A

E

E

I

I

W

L

E

W

Q

Q

T

L

D

D

G

N

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K

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V

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D

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M

W

I

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V

A

V

A

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T
x
A

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|
G

T
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T

G
x
A

G

G

T
|
T

F

I

A

S

G

G

V

I

S

G

L
x
R

F

K

L

I

K

K

E

E

K

Q

N

V

P

P

Q

S

I

C

K

Q

T

I

V

V

L

G

A

V

D

D

P

P

M

Y

G

G

S

S

G

I

L

L

Y

A

S

R

Y

P

V

A

K

E

T

L

G

N

E

K

I

T

S

D

S

V

E

Q

G

F

N

Y

S

E

I

V

T

-

E

E

G
|
G

I
|
I

G

G

N

Y

S

D

R

F

I

P

T

P

K

T

N

V

M

F

E

D

N

D

V

T

M

V

I

V

D

D

D

V

A

W

I

T

R

K

V

I

D

G

D

D

K

S

E

D

A

C

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F

R

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M

V

S

Y

R

Q

R

L

L

L

N

R

A

K

E

D

E

G

G

L

L

F

L

M

C

G

G

S
|
S

V

S

G

G

I

G

N

A

V

M

G

H

A

A

V

L

A

E

L

H

A

A

K

R

Q

K

M

L

G

K

P

K

G

G

H

Q

T

R

I

C

V

V

T

V

V

I

L

L

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x
P

D
|
D

S

G

G

I

T

R

R

N

Y

Y

Q

M

S

T

K

K

L

F

F

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S

R

D

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N

W

W

L

M

A

E

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R

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L

F

active site: K82 (= K44), S312 (= S274)
binding protoporphyrin ix containing fe: A189 (≠ L150), P192 (≠ R153), L193 (≠ I154), Y196 (= Y157), R229 (≠ L190)
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 (= Q146), A218 (≠ T179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (= T184), G268 (= G230), I269 (= I231), S312 (= S274), P338 (≠ C300), D339 (= D301)

Sites not aligning to the query:

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

P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 96% coverage: 11:322/326 of query aligns to 11:317/464 of P9WP51

query
sites
P9WP51

V

I

G

G

N

G

T

T

P

P

L

L

I

V

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R

L

L

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F

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V

E

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E

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C

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A

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A

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A

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L

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A

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Y

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G

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A

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E

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C

P

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-

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A

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N

D

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P

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A

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A

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A

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A

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A

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N

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G

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-

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A

A

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L

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Y

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Y

-

V

-

K

-

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-

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-

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-

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-

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E

A

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N

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P

-

Y

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L

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A

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A

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E

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A

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I

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F

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A

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W

L

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A

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N

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L

L

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)
41% identity, 96% coverage: 11:322/326 of query aligns to 9:315/458 of 7xoyA

query
sites
7xoyA

V

I

G

G

N

G

T

T

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L

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R

L

L

N

N

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G

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G

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T

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V

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A

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A

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K

A

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|
K

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A

A

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I

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K

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A

A

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L

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K

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P

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A
x
S

G

G

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|
N

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|
T

G

G

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G

G

L

L

A

A

H

L

I

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C

A

N

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|
T

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A

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-

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A

A

D

D

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M

E

G

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-

L

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Y

-

V

-

K

-

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-

G

-

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-

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-

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-

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I

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K

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D

A

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R

D

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M

V

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Y

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L

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A

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K

E

D

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G

A

L

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F

L

M

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|
S

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C

G

G

I

M

N

A

V

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G

V

A

A

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L

A

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L

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A

A

K

E

Q

E

M

A

G

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A

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I

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V

V

L

L

L

C
x
P

D

D

S

G

G

G

T

R

R

G

Y

Y

Q

M

S

S

K

K

L

I

F

F

N

N

R

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A

W

W

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M

A

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S

K

Y

N

G

L

F

L

L

binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: K42 (= K44), S70 (≠ A72), N72 (= N74), T73 (= T75), T180 (= T181), G182 (= G183), T183 (= T184), S267 (= S274), P293 (≠ C300)

7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
41% identity, 96% coverage: 11:322/326 of query aligns to 9:315/458 of 7xnzB

query
sites
7xnzB

V

I

G

G

N

G

T

T

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P

L

L

I

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R

L

L

N

N

S

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G

G

A

C

G

E

T

I

V

L

A

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A

K

K

A

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E

E

F

Y

L

L

N

N

P

P

G

G

S

S

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K
|
K

D

D

R

R

A

I

A

A

L

V

Y

K

I

M

I

I

K

E

D

A

A

A

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E

E

A

K

S

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G

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L

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K

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P

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Y

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A

L

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G

G

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P

-

T

A

A

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A

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Y

Y

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M

V

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S

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D

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L

A

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I

I

E

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N

G

A

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Q

F

Y

D

A

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N

L

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A

A

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G
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T

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G

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T

F

I

A

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G

G

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A

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G

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Y

L

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K

E

E

-

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A

A

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-

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K

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I

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S

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C

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G

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M

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A

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x
P

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|
D

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G

G

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R

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Y

Y

Q

M

S

S

K

K

L

I

F

F

N

N

R

D

E

A

W

W

L

M

A

S

T

S

K

Y

N

G

L

F

L

L

binding pyridoxal-5'-phosphate: K42 (= K44), G179 (= G180), T180 (= T181), G181 (= G182), G182 (= G183), T183 (= T184), S267 (= S274), P293 (≠ C300), D294 (= D301)

6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
36% identity, 98% coverage: 8:325/326 of query aligns to 13:333/468 of 6xylA

query
sites
6xylA

I

L

G

D

T

A

V

I

G

G

N

N

T

T

P

P