SitesBLAST

P78 (= P8) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
G85 (= G15) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T17) 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 (= C37) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P42) 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 (= K47) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ A53) 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 (≠ I54) to V: in CBSD; loss of activity
E131 (= E59) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G67) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ V71) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E72) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G76) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N77) binding pyridoxal 5'-phosphate
L154 (= L82) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A83) 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 (≠ T93) 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 (≠ Q101) 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 (= E104) 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 (≠ T108) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ V119) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ A138) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ T153) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N155) 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 (= A158) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ R161) 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 183:187) binding pyridoxal 5'-phosphate
T257 (= T184) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ A189) 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 (≠ L193) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K196) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ S199) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ V202) 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 (≠ G205) 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 (= D208) to N: in CBSD; loss of activity
A288 (≠ F215) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ S229) 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 (= G233) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G235) 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 (= V248) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D249) to V: in CBSD; loss of activity
R336 (≠ I264) 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 (= L266) 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 (= G275) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S277) 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 (≠ N281) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ T297) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D304) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ M307) 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 (≠ S312) 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

4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
43% identity, 96% coverage: 6:324/332 of query aligns to 34:352/486 of 4pcuA

query
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active site: K77 (= K47), S105 (≠ A75), D237 (= D208), S305 (= S277)
binding protoporphyrin ix containing fe: A182 (≠ T153), P185 (≠ R156), L186 (= L157), Y189 (≠ I160), R222 (≠ L193), T269 (≠ A241)
binding pyridoxal-5'-phosphate: K77 (= K47), N107 (= N77), G212 (= G183), T213 (= T184), G214 (= G185), T216 (= T187), G261 (= G233), S305 (= S277), P331 (≠ C303), D332 (= D304)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479

1jbqA Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate dependent hemeprotein (see paper)
43% identity, 96% coverage: 6:324/332 of query aligns to 34:347/348 of 1jbqA

query
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1jbqA

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active site: K77 (= K47), S105 (≠ A75), D232 (= D208), S236 (≠ A212), L238 (= L214), S300 (= S277), P326 (≠ C303)
binding protoporphyrin ix containing fe: A177 (≠ T153), P180 (≠ R156), L181 (= L157), Y184 (≠ I160), R217 (≠ L193)
binding pyridoxal-5'-phosphate: K77 (= K47), N107 (= N77), V206 (= V182), G207 (= G183), T208 (= T184), G209 (= G185), G210 (= G186), T211 (= T187), G256 (= G233), S300 (= S277), P326 (≠ C303), D327 (= D304)

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)
41% identity, 97% coverage: 6:328/332 of query aligns to 35:358/504 of Q2V0C9

query
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Q2V0C9

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T

K

Q

M

S

S

Q

D

E

E

K

K

Q

I

D

S

T

T

L

L

R

Y

A

A

L

L

G

G

A

A

E

K

L

I

V

I

L

R

V

T

P

P

P

T

T

E

A

A

-

S

Y

W

S

H

N

S

P

P

A

E

H

A

Y

H

V

I

H

S

T

V

S

A

R

Q

R

K

I

L

A

Q

E

K

E

E

T

I

P

P

G

N

A

S

L

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

T

P

A

G

N

N

R

P

L

L

A

A

H

H

I

Y

R

D

T

Q

T

T

A

A

P

I

E

E

I

I

W

W

A

K

Q

Q

T

C

G

E

G

G

R

K

I

I

D

D

G

Y

F

L

T

V

C

A

A

G

V

A

G
|
G

T
|
T

G
|
G

T
|
T

L

I

A

S

G

G

V

I

G

G

L

R

G

K

L

L

K

K

A

E

F

L

S

S

E

P

D

N

V

I

V

K

I

I

G

I

L

A

T

V

D

D

P

P

Y

K

G

G

A

S

A

I

L

L

F

D

N

P

Y

-

F

-

A

S

H

S

G

D

E

S

L

Q

K

N

A

E

E

V

G

G

S

F

S

Y

V

E

A

V

E

E

G

G

I

I

G

G

Q

Y

S

D

R

F

I

I

T

P

A

T

N

V

L

L

D

D

G

R

A

N

P

V

V

I

D

D

T

K

Q

W

F

I

R

K

V

T

S

E

D

D

E

N

E

E

G

S

L

L

E

N

Q

A

V

A

I

R

A

M

L

L

L

I

G

R

S

Q

E

E

G

G

L

L

C

L

V

C

G

G

L

G

S
|
S

S

S

G

G

I

A

N

A

V

L

A

I

G

A

A

A

I

L

A

K

L

I

A

A

K

K

E

D

L

I

G

P

P

E

G

E

K

K

T

R

I

M

V

V

T

I

I

I

L

L

C

P

D

D

S

G

G

I

M

R

R

N

Y

Y

L

L

S

T

S

K

L

F

F

V

N

S

P

E

A

Y

W

W

L

M

E

E

A

T

K

R

G

G

L

F

P

L

V

Q

P

P

A

V

K78 (= K47) modified: N6-(pyridoxal phosphate)lysine
N108 (= N77) binding pyridoxal 5'-phosphate
GTGGT 215:219 (= GTGGT 183:187) binding pyridoxal 5'-phosphate
S307 (= S277) 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)
41% identity, 97% coverage: 6:328/332 of query aligns to 31:351/488 of 5ohxA

query
sites
5ohxA

I

I

A

M

P

P

D

D

A

I

L

L

A

T

L

A

I

I

G

G

N

Q

T

T

P

P

L

L

V

I

R

K

L

L

K

N

G

N

P

I

S

P

E

K

A

S

T

Y

G

G

-

I

-

K

C

C

E

E

I

I

L

Y

A

A

K

K

C

C

E

E

F

F

M

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

A

L

Y

A

R

I

M

I

I

T

Q

D

D

A

A

E

E

E

D

R

K

G

G

L

L

I

L

A

K

P

P

G

G

G

C

I

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

G

A

N

A

A

V

R

R

G

G

Y

Y

R

K

T

C

I

I

V

V

M

M

T

P

D

E

T

K

Q

M

S

S

Q

D

E

E

K

K

Q

I

D

S

T

T

L

L

R

Y

A

A

L

L

G

G

A

A

E

K

L

I

V

I

L

R

V

T

P

P

P

T

T

E

A

A

-

S

Y

W

S

H

N

S

P

P

A

E

H

A

Y

H

V

I

H

S

T

V

S

A

R

Q

R

K

I

L

A

Q

E

K

E

E

T

I

P

P

G

N

A

S

L

I

W

I

A

L

N

D

Q

Q

F

Y

D

T

N

N

T
x
P

A

G

N

N

R
x
P

L

L

A

A

H

H

I
x
Y

R

D

T

Q

T

T

A

A

P

I

E

E

I

I

W

W

A

K

Q

Q

T

C

G

E

G

G

R

K

I

I

D

D

G

Y

F

L

T

V

C

A

A
x
G

V

A

G
|
G

T
|
T

G
|
G

T
|
T

L

I

A

S

G

G

V

I

G

G

L
x
R

G

K

L

L

K

K

A

E

F

L

S

S

E

P

D

N

V

I

V

K

I

I

G

I

L

A

T

V

D

D

P

P

Y

K

G

G

A

S

A

I

L

L

F

-

N

-

Y

-

F

-

A

-

H

D

G

P

E

S

L

S

K

D

A

E

E

V

G

G

S

F

S

Y

V

E

A

V

E

E

G
|
G

I

I

G

G

Q

Y

S

D

R

F

I

I

T

P

A

T

N

V

L

L

D

D

G

R

A

N

P

V

V

I

D

D

T

K

Q

W

F

I

R

K

V

T

S

E

D

D

E

N

E

E

G

S

L

L

E

N

Q

A

V

A

I

R

A

M

L

L

L

I

G

R

S

Q

E

E

G

G

L

L

C

L

V

C

G

G

L

G

S
|
S

S

S

G

G

I

A

N

A

V

L

A

I

G

A

A

A

I

L

A

K

L

I

A

A

K

K

E

D

L

I

G

P

P

E

G

E

K

K

T

R

I

M

V

V

T

I

I

I

L

L

C
x
P

D
|
D

S

G

G

I

M

R

R

N

Y

Y

L

L

S

T

S

K

L

F

F

V

N

S

P

E

A

Y

W

W

L

M

E

E

A

T

K

R

G

G

L

F

P

L

V

Q

P

P

A

V

binding protoporphyrin ix containing fe: P181 (≠ T153), P184 (≠ R156), Y188 (≠ I160), R221 (≠ L193)
binding pyridoxal-5'-phosphate: K74 (= K47), N104 (= N77), G209 (≠ A181), G211 (= G183), T212 (= T184), G213 (= G185), G214 (= G186), T215 (= T187), G256 (= G233), S300 (= S277), P326 (≠ C303), D327 (= D304)

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)
37% identity, 98% coverage: 1:327/332 of query aligns to 33:362/504 of 3pc4A

query
sites
3pc4A

M

I

A

A

H

H

-

R

D

Q

M

Q

I

I

A

T

P

P

D

N

A

I

L

L

A

E

L

V

I

I

G

G

N

C

T

T

P

P

L

L

V

V

R

K

L

L

K

N

G

N

-

I

-

P

P

A

S

S

E

D

A

G

T

I

G

E

C

C

E

E

I

M

L

Y

A

A

K

K

C

C

E

E

F

F

M

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

A

R

I

M

I

V

T

Q

D

D

A

A

E

E

R

Q

G

G

L

L

I

L

A

K

P

P

G

G

G

Y

I

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

G

C

N

A

A

V

R

K

G

G

Y

Y

R

K

T

C

I

I

V

V

M

M

T

P

D

E

T

K

Q

M

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S

Q

N

E

E

K

K

Q

V

D

S

T

A

L

L

R

R

A

T

L

L

G

G

A

A

E

K

L

I

V

I

L

R

V

T

P

P

-

T

P

E

T

A

A

A

Y

Y

S

D

N

S

P

P

A

E

H

G

Y

L

V

I

H

Y

T

V

S

A

R

Q

I

L

A

Q

E

R

E

E

T

T

P

P

G

N

A

S

L

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

T
x
A

A

G

N

N

R
x
P

L
|
L

A

A

H

H

I
x
Y

R

D

T

G

T

T

A

A

P

A

E

E

I

I

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L

A

W

Q

Q

T

L

G

D

G

N

R

K

I

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F

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x
A

G
|
G

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x
A

G

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T
|
T

L

I

A

S

G

G

V

I

G

G

L
x
R

G

K

L

I

K

K

A

E

F

Q

S

V

E

P

D

S

V

C

V

Q

I

I

G

V

L

G

T

V

D

D

P

P

Y

Y

G

G

A

S

A

I

L

L

F

A

N

R

Y

P

F

A

A

E

H

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

V

V

A

-

E

E

G
|
G

I
|
I

G

G

Q
x
Y

S

D

R

F

I

P

T

P

A
x
T

N

V

L

F

D

D

G

D

A

T

P

V

V

V

D

D

T

V

Q

W

F

T

R

K

V

I

S

G

D

D

E

S

E

D

G

C

L

F

E

P

Q

M

V

S

I

R

A

R

L

L

L

N

G

A

S

E

E

E

G

G

L

L

C

L

V

C

G

G

L

G

S
|
S

S

S

G

G

I

G

N

A

V

M

A

H

G

A

A

A

I

L

A

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

K

Q

T

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

S

G

G

I

M

R

R

N

Y

Y

L

M

S

T

S

K

L

F

F

V

N

S

P

D

A

N

W

W

L

M

E

E

A

A

K

R

G

N

L

F

P

K

V

E

P

P

active site: K82 (= K47), S312 (= S277)
binding protoporphyrin ix containing fe: A189 (≠ T153), P192 (≠ R156), L193 (= L157), Y196 (≠ I160), R229 (≠ L193), T276 (≠ A241)
binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K47), T109 (= T74), S110 (≠ A75), N112 (= N77), T113 (= T78), Q185 (= Q149), A218 (≠ V182), G219 (= G183), T220 (= T184), A221 (≠ G185), T223 (= T187), G268 (= G233), I269 (= I234), Y271 (≠ Q236), S312 (= S277), P338 (≠ C303), D339 (= D304)

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)
37% identity, 98% coverage: 1:327/332 of query aligns to 33:362/504 of 3pc3A

query
sites
3pc3A

M

I

A

A

H

H

-

R

D

Q

M

Q

I

I

A

T

P

P

D

N

A

I

L

L

A

E

L

V

I

I

G

G

N

C

T

T

P

P

L

L

V

V

R

K

L

L

K

N

G

N

-

I

-

P

P

A

S

S

E

D

A

G

T

I

G

E

C

C

E

E

I

M

L

Y

A

A

K

K

C

C

E

E

F

F

M

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

A

R

I

M

I

V

T

Q

D

D

A

A

E

E

R

Q

G

G

L

L

I

L

A

K

P

P

G

G

G

Y

I

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

G

C

N

A

A

V

R

K

G

G

Y

Y

R

K

T

C

I

I

V

V

M

M

T

P

D

E

T

K

Q

M

S

S

Q

N

E

E

K

K

Q

V

D

S

T

A

L

L

R

R

A

T

L

L

G

G

A

A

E

K

L

I

V

I

L

R

V

T

P

P

-

T

P

E

T

A

A

A

Y

Y

S

D

N

S

P

P

A

E

H

G

Y

L

V

I

H

Y

T

V

S

A

R

Q

I

L

A

Q

E

R

E

E

T

T

P

P

G

N

A

S

L

I

W

V

A

L

N

D

Q
|
Q

F

Y

D

R

N

N

T
x
A

A

G

N

N

R
x
P

L
|
L

A

A

H

H

I
x
Y

R

D

T

G

T

T

A

A

P

A

E

E

I

I

W

L

A

W

Q

Q

T

L

G

D

G

N

R

K

I

V

D

D

G

M

F

I

T

V

C

V

A

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

L

I

A

S

G

G

V

I

G

G

L
x
R

G

K

L

I

K

K

A

E

F

Q

S

V

E

P

D

S

V

C

V

Q

I

I

G

V

L

G

T

V

D

D

P

P

Y

Y

G

G

A

S

A

I

L

L

F

A

N

R

Y

P

F

A

A

E

H

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

V

V

A

-

E

E

G
|
G

I
|
I

G

G

Q

Y

S

D

R

F

I

P

T

P

A

T

N

V

L

F

D

D

G

D

A

T

P

V

V

V

D

D

T

V

Q

W

F

T

R

K

V

I

S

G

D

D

E

S

E

D

G

C

L

F

E

P

Q

M

V

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I

R

A

R

L

L

L

N

G

A

S

E

E

E

G

G

L

L

C

L

V

C

G

G

L

G

S
|
S

S

S

G

G

I

G

N

A

V

M

A

H

G

A

A

A

I

L

A

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

K

Q

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R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

S

G

G

I

M

R

R

N

Y

Y

L

M

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K

L

F

F

V

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N

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A

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P

P

active site: K82 (= K47), S312 (= S277)
binding protoporphyrin ix containing fe: A189 (≠ T153), P192 (≠ R156), L193 (= L157), Y196 (≠ I160), R229 (≠ L193)
binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K47), T109 (= T74), S110 (≠ A75), N112 (= N77), T113 (= T78), Q185 (= Q149), A218 (≠ V182), G219 (= G183), T220 (= T184), A221 (≠ G185), T223 (= T187), G268 (= G233), I269 (= I234), S312 (= S277), P338 (≠ C303), D339 (= D304)

Sites not aligning to the query:

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

3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
37% identity, 98% coverage: 1:327/332 of query aligns to 31:360/500 of 3pc2A

query
sites
3pc2A

M

I

A

A

H

H

-

R

D

Q

M

Q

I

I

A

T

P

P

D

N

A

I

L

L

A

E

L

V

I

I

G

G

N

C

T

T

P

P

L

L

V

V

R

K

L

L

K

N

G

N

-

I

-

P

P

A

S

S

E

D

A

G

T

I

G

E

C

C

E

E

I

M

L

Y

A

A

K

K

C

C

E

E

F

F

M

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

Y

A

R

I

M

I

V

T

Q

D

D

A

A

E

E

R

Q

G

G

L

L

I

L

A

K

P

P

G

G

G

Y

I

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

G

C

N

A

A

V

R

K

G

G

Y

Y

R

K

T

C

I

I

V

V

M

M

T

P

D

E

T

K

Q

M

S

S

Q

N

E

E

K

K

Q

V

D

S

T

A

L

L

R

R

A

T

L

L

G

G

A

A

E

K

L

I

V

I

L

R

V

T

P

P

-

T

P

E

T

A

A

A

Y

Y

S

D

N

S

P

P

A

E

H

G

Y

L

V

I

H

Y

T

V

S

A

R

Q

I

L

A

Q

E

R

E

E

T

T

P

P

G

N

A

S

L

I

W

V

A

L

N

D

Q

Q

F

Y

D

R

N

N

T
x
A

A

G

N

N

R
x
P

L
|
L

A

A

H

H

I
x
Y

R

D

T

G

T

T

A

A

P

A

E

E

I

I

W

L

A

W

Q

Q

T

L

G

D

G

N

R

K

I

V

D

D

G

M

F

I

T

V

C

V

A

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

L

I

A

S

G

G

V

I

G

G

L
x
R

G

K

L

I

K

K

A

E

F

Q

S

V

E

P

D

S

V

C

V

Q

I

I

G

V

L

G

T

V

D

D

P

P

Y

Y

G

G

A

S

A

I

L

L

F

A

N

R

Y

P

F

A

A

E

H

L

G

N

E

K

L

T

K

D

A

V

E

Q

G

F

S

Y

S

E

V

V

A

-

E

E

G
|
G

I

I

G

G

Q

Y

S

D

R

F

I

P

T

P

A

T

N

V

L

F

D

D

G

D

A

T

P

V

V

V

D

D

T

V

Q

W

F

T

R

K

V

I

S

G

D

D

E

S

E

D

G

C

L

F

E

P

Q

M

V

S

I

R

A

R

L

L

L

N

G

A

S

E

E

E

G

G

L

L

C

L

V

C

G

G

L

G

S
|
S

S

S

G

G

I

G

N

A

V

M

A

H

G

A

A

A

I

L

A

E

L

H

A

A

K

R

E

K

L

L

G

K

P

K

G

G

K

Q

T

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

S

G

G

I

M

R

R

N

Y

Y

L

M

S

T

S

K

L

F

F

V

N

S

P

D

A

N

W

W

L

M

E

E

A

A

K

R

G

N

L

F

P

K

V

E

P

P

active site: K80 (= K47), S310 (= S277)
binding protoporphyrin ix containing fe: A187 (≠ T153), P190 (≠ R156), L191 (= L157), Y194 (≠ I160), R227 (≠ L193)
binding pyridoxal-5'-phosphate: K80 (= K47), N110 (= N77), A216 (≠ V182), G217 (= G183), T218 (= T184), A219 (≠ G185), T221 (= T187), G266 (= G233), S310 (= S277), P336 (≠ C303), D337 (= D304)

Sites not aligning to the query:

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

6xylA Crystal structure of delta466-491 cystathionine beta-synthase from toxoplasma gondii with l-serine (see paper)
38% identity, 96% coverage: 6:324/332 of query aligns to 8:329/468 of 6xylA

query
sites
6xylA

I

I

A

L

P

D

D

S

A

V

L

L

A

D

L

A

I

I

G

G

N

N

T

T

P

P

L

M

V

V

R

R

L

M

K

K

G

R

P

L

S

A

E

K

A

V

T

Y

G

G

-

L

-

E

C

C

E

D

I

L

L

L

A

A

K

K

C

C

E

E

F

F

M

M

N

S

P

A

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

K

A

A

I

M

I

V

T

E

D

K

A

A

E

E

E

R

R

E

G

G

L

R

I

L

A

K

P

A

G

G

G

D

I

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

G

A

N

A

A

V

R

R

G

G

Y

Y

R

R

T

M

I

I

I

V

V

T

M

M

T

P

D

A

T

K

Q

M

S

S

Q

A

E

E

K

K

Q

S

D

N

T

I

L

M

R

K

A

C

L

L

G

G

A

A

E

E

L

I

V

V

L

R

V

T

P

P

-

T

P

E

T

A

A

A

Y

W

S

N

N

D

P

E

A

N

H

S

Y

H

V

M

H

G

T

V

S

A

R

A

R

K

I

L

A

Q

E

R

E

E

T

L

P

E

G

N

A

A

L

H

W

I

A

L

N

D

Q
|
Q

F

Y

D

N

N

N

T

T

A

A

N

N

R

P

L

M

A

V

H

H

I

Y

R

D

T

V

T

T

A

A

P

E

E

E

I

I

W

I

A

T

Q

Q

T

C

G

D

G

G

R

D

I

I

D

D

G

M

F

V

T

V

C

I

A

G

V

A

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

A

T

G

G

V

I

G

G

L

R

G

K

L

I

K

K

A

E

F

R

S

C

E

P

D

K

V

C

V

K

I

V

G

V

L

G

T

V

D

D

P

P

Y

K

G

G

A

S

A

I

L

L

F

A

N

V

Y

P

F

D

A

S

H

L

G

N

E

D

L

E

K

K

A

R

E

L

G

Q

S

S

S

Y

V

E

A

V

E

E

G
|
G

I
|
I

G

G

Q
x
Y

S

D

R

F

I

V

T

P

A

G

N

V

L

L

D

D

G

R

A

K

P

V

V

V

D

D

T

E

Q

W

F

V

R

K

V

V

S

G

D

D

E

A

E

E

G

S

L

F

E

T

Q

T

V

A

I

R

A

A

L

I

G

R

S

N

E

E

G

G

L

L

C

F

V

V

G

G

L

G

S
|
S

S

S

G

G

I

A

N

N

V

V

A

W

G

G

A

A

I

L

A

Q

L

A

A

A

K

R

E

Q

L

L

G

K

P

K

G

G

K

Q

T

K

I

C

V

V

T

V

I

L

L

L

C
x
P

D
|
D

S

S

G

S

M

R

R

N

Y

Y

L

M

S

S

S

K

L

F

F

I

N

S

P

D

A

E

W

W

L

M

E

A

A

E

K

H

G

G

L

F

binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K51 (= K47), T82 (= T78), Q154 (= Q149), G188 (= G183), T189 (= T184), G190 (= G185), T192 (= T187), G238 (= G233), I239 (= I234), Y241 (≠ Q236), S282 (= S277), P308 (≠ C303), D309 (= D304)

6xwlC Cystathionine beta-synthase from toxoplasma gondii (see paper)
38% identity, 96% coverage: 6:324/332 of query aligns to 8:329/477 of 6xwlC

query
sites
6xwlC

I

I

A

L

P

D

D

S

A

V

L

L

A

D

L

A

I

I

G

G

N

N

T

T

P

P

L

M

V

V

R

R

L

M

K

K

G

R

P

L

S

A

E

K

A

V

T

Y

G

G

-

L

-

E

C

C

E

D

I

L

L

L

A

A

K

K

C

C

E

E

F

F

M

M

N

S

P

A

G

G

S

S

V

V

K
|
K

D

D

R

R

A

I

A

G

L

K

A

A

I

M

I

V

T

E

D

K

A

A

E

E

E

R

R

E

G

G

L

R

I

L

A

K

P

A

G

G

G

D

I

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

G

A

N

A

A

V

R

R

G

G

Y

Y

R

R

T

M

I

I

I

V

V

T

M

M

T

P

D

A

T

K

Q

M

S

S

Q

A

E

E

K

K

Q

S

D

N

T

I

L

M

R

K

A

C

L

L

G

G

A

A

E

E

L

I

V

V

L

R

V

T

P

P

-

T

P

E

T

A

A

A

Y

W

S

N

N

D

P

E

A

N

H

S

Y

H

V

M

H

G

T

V

S

A

R

A

R

K

I

L

A

Q

E

R

E

E

T

L

P

E

G

N

A

A

L

H

W

I

A

L

N

D

Q

Q

F

Y

D

N

N

N

T

T

A

A

N

N

R

P

L

M

A

V

H

H

I

Y

R

D

T

V

T

T

A

A

P

E

E

E

I

I

W

I

A

T

Q

Q

T

C

G

D

G

G

R

D

I

I

D

D

G

M

F

V

T

V

C

I

A

G

V

A

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

A

T

G

G

V

I

G

G

L

R

G

K

L

I

K

K

A

E

F

R

S

C

E

P

D

K

V

C

V

K

I

V

G

V

L

G

T

V

D

D

P

P

Y

K

G

G

A

S

A

I

L

L

F

A

N

V

Y

P

F

D

A

S

H

L

G

N

E

D

L

E

K

K

A

R

E

L

G

Q

S

S

S

Y

V

E

A

V

E

E

G
|
G

I

I

G

G

Q

Y

S

D

R

F

I

V

T

P

A

G

N

V

L

L

D

D

G

R

A

K

P

V

V

V

D

D

T

E

Q

W

F

V

R

K

V

V

S

G

D

D

E

A

E

E

G

S

L

F

E

T

Q

T

V

A

I

R

A

A

L

I

G

R

S

N

E

E

G

G

L

L

C

F

V

V

G

G

L

G

S
|
S

S

S

G

G

I

A

N

N

V

V

A

W

G

G

A

A

I

L

A

Q

L

A

A

A

K

R

E

Q

L

L

G

K

P

K

G

G

K

Q

T

K

I

C

V

V

T

V

I

L

L

L

C
x
P

D
|
D

S

S

G

S

M

R

R

N

Y

Y

L

M

S

S

S

K

L

F

F

I

N

S

P

D

A

E

W

W

L

M

E

A

A

E

K

H

G

G

L

F

binding pyridoxal-5'-phosphate: K51 (= K47), N81 (= N77), G188 (= G183), T189 (= T184), G190 (= G185), T192 (= T187), G238 (= G233), S282 (= S277), P308 (≠ C303), D309 (= D304)

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
43% identity, 90% coverage: 14:312/332 of query aligns to 7:298/302 of 2efyA

query
sites
2efyA

I

I

G

G

N

K

T

T

P

P

L

V

V

V

R

R

L

L

K

A

G

K

P

V

S

V

E

E

A

P

T

D

G

M

C

A

E

E

I

V

L

W

A

V

K

K

C

L

E

E

F

G

M

L

N

N

P

P

G

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

A

Y

I

M

I

I

T

K

D

D

A

A

E

E

R

R

G

G

L

I

I

L

A

R

P

P

G

G

G

S

-

G

-

Q

I

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

G

A

N

A

A

S

R

R

G

G

Y

Y

R

R

T

L

I

I

I

L

V

T

M

M

T

P

D

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

Q

K

D

R

T

V

L

L

R

K

A

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

V

T

P

D

P

P

T

E

A

R

Y

R

S

M

N

L

P

A

A

A

H

R

Y

-

V

-

H

E

T

E

S

A

R

L

R

R

I

L

A

K

E

E

T

L

P

-

G

G

A

A

L

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

T

P

A

A

N

N

R

V

L

R

A

A

H

H

I

Y

R

E

T

T

A

G

P

P

E

E

I

L

W

Y

A

E

Q

A

T

L

G

E

G

G

R

R

I

I

D

D

G

A

F

F

T

V

C
x
Y

A

G

V

S

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

A

T

G

G

V

V

G

G

L

R

G

Y

L

L

K

K

A

E

F

R

S

I

E

P

D

H

V

V

V

K

I

V

G

I

L

A

T

V

D
x
E

P

P

Y

-

G

-

A

-

A

A

L

R

F
x
S

N

N

Y

V

F

L

A

S

H

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

F

S

-

V

-

A

-

E

Q

G
|
G

I
x
M

G

G

Q
x
P

S

G

R

F

I

I

T

P

A

E

N

N

L

L

D

D

G

L

A

S

P

L

V

L

D

D

T

G

Q

V

F

I

R

Q

V

V

S

W

D

E

E

E

E

D

G

A

L

F

E

P

Q

L

V

A

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

G

L

L

C

F

V

L

G

G

L

M

S
|
S

S

S

G

G

I

G

N

I

V

V

A

W

G

A

A

A

I

L

A

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

K

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D
|
D

S

G

G

G

M

W

R

K

Y

Y

L

L

S

S

S

T

active site: K40 (= K47), S70 (≠ A75), E200 (≠ D208), S204 (≠ F215), S263 (= S277)
binding 5-oxohexanoic acid: T69 (= T74), G71 (= G76), T73 (= T78), Q141 (= Q149), G175 (= G183), G219 (= G233), M220 (≠ I234), P222 (≠ Q236)
binding pyridoxal-5'-phosphate: K40 (= K47), N72 (= N77), Y172 (≠ C180), G175 (= G183), T176 (= T184), G177 (= G185), T179 (= T187), G219 (= G233), S263 (= S277), P289 (≠ C303), D290 (= D304)

2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
43% identity, 90% coverage: 14:312/332 of query aligns to 7:298/302 of 2ecqA

query
sites
2ecqA

I

I

G

G

N

K

T

T

P

P

L

V

V

V

R

R

L

L

K

A

G

K

P

V

S

V

E

E

A

P

T

D

G

M

C

A

E

E

I

V

L

W

A

V

K

K

C

L

E

E

F

G

M

L

N

N

P

P

G

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

A

Y

I

M

I

I

T

K

D

D

A

A

E

E

R

R

G

G

L

I

I

L

A

R

P

P

G

G

G

S

-

G

-

Q

I

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

G

A

N

A

A

S

R

R

G

G

Y

Y

R

R

T

L

I

I

I

L

V

T

M

M

T

P

D

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

Q

K

D

R

T

V

L

L

R

K

A

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

V

T

P

D

P

P

T

E

A

R

Y

R

S

M

N

L

P

A

A

A

H

R

Y

-

V

-

H

E

T

E

S

A

R

L

R

R

I

L

A

K

E

E

T

L

P

-

G

G

A

A

L

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

T

P

A

A

N

N

R

V

L

R

A

A

H

H

I

Y

R

E

T

T

A

G

P

P

E

E

I

L

W

Y

A

E

Q

A

T

L

G

E

G

G

R

R

I

I

D

D

G

A

F

F

T

V

C
x
Y

A
x
G

V

S

G
|
G

T
|
T

G

G

T
|
T

L

I

A

T

G

G

V

V

G

G

L

R

G

Y

L

L

K

K

A

E

F

R

S

I

E

P

D

H

V

V

V

K

I

V

G

I

L

A

T

V

D
x
E

P

P

Y

-

G

-

A

-

A

A

L

R

F
x
S

N

N

Y

V

F

L

A

S

H

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

F

S

-

V

-

A

-

E

Q

G
|
G

I

M

G

G

Q

P

S

G

R

F

I

I

T

P

A

E

N

N

L

L

D

D

G

L

A

S

P

L

V

L

D

D

T

G

Q

V

F

I

R

Q

V

V

S

W

D

E

E

E

E

D

G

A

L

F

E

P

Q

L

V

A

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

G

L

L

C

F

V

L

G

G

L

M

S
|
S

S

S

G

G

I

G

N

I

V

V

A

W

G

A

A

A

I

L

A

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

K

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D

D

S

G

G

G

M

W

R

K

Y

Y

L

L

S

S

S

T

active site: K40 (= K47), S70 (≠ A75), E200 (≠ D208), S204 (≠ F215), S263 (= S277)
binding (3s)-3-hydroxybutanoic acid: K40 (= K47), G71 (= G76), T73 (= T78), Q141 (= Q149), G219 (= G233)
binding pyridoxal-5'-phosphate: K40 (= K47), N72 (= N77), Y172 (≠ C180), G173 (≠ A181), G175 (= G183), T176 (= T184), T179 (= T187), G219 (= G233), S263 (= S277), P289 (≠ C303)

2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
43% identity, 90% coverage: 14:312/332 of query aligns to 7:298/302 of 2ecoA

query
sites
2ecoA

I

I

G

G

N

K

T

T

P

P

L

V

V

V

R

R

L

L

K

A

G

K

P

V

S

V

E

E

A

P

T

D

G

M

C

A

E

E

I

V

L

W

A

V

K

K

C

L

E

E

F

G

M

L

N

N

P

P

G

G

S

S

V

I

K
|
K

D

D

R

R

A

P

A

A

L

W

A

Y

I

M

I

I

T

K

D

D

A

A

E

E

R

R

G

G

L

I

I

L

A

R

P

P

G

G

G

S

-

G

-

Q

I

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

G

A

N

A

A

S

R

R

G

G

Y

Y

R

R

T

L

I

I

I

L

V

T

M

M

T

P

D

A

T

Q

Q

M

S

S

Q

E

E

E

K

R

Q

K

D

R

T

V

L

L

R

K

A

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

V

T

P

D

P

P

T

E

A

R

Y

R

S

M

N

L

P

A

A

A

H

R

Y

-

V

-

H

E

T

E

S

A

R

L

R

R

I

L

A

K

E

E

T

L

P

-

G

G

A

A

L

F

W

M

A

P

N

D

Q
|
Q

F

F

D

K

N

N

T

P

A

A

N

N

R

V

L

R

A

A

H

H

I

Y

R

E

T

T

A

G

P

P

E

E

I

L

W

Y

A

E

Q

A

T

L

G

E

G

G

R

R

I

I

D

D

G

A

F

F

T

V

C
x
Y

A

G

V

S

G
|
G

T
|
T

G

G

T
|
T

L

I

A

T

G

G

V

V

G

G

L

R

G

Y

L

L

K

K

A

E

F

R

S

I

E

P

D

H

V

V

V

K

I

V

G

I

L

A

T

V

D
x
E

P

P

Y

-

G

-

A

-

A

A

L

R

F
x
S

N

N

Y

V

F

L

A

S

H

G

G

G

E

K

L

M

K

G

A

Q

E

H

G

G

S

F

S

-

V

-

A

-

E

Q

G
|
G

I

M

G

G

Q

P

S

G

R

F

I

I

T

P

A

E

N

N

L

L

D

D

G

L

A

S

P

L

V

L

D

D

T

G

Q

V

F

I

R

Q

V

V

S

W

D

E

E

E

E

D

G

A

L

F

E

P

Q

L

V

A

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

G

L

L

C

F

V

L

G

G

L

M

S
|
S

S

S

G

G

I

G

N

I

V

V

A

W

G

A

A

A

I

L

A

Q

L

V

A

A

K

R

E

E

L

L

G

G

P

P

G

G

K

K

T

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D
|
D

S

G

G

G

M

W

R

K

Y

Y

L

L

S

S

S

T

active site: K40 (= K47), S70 (≠ A75), E200 (≠ D208), S204 (≠ F215), S263 (= S277)
binding 4-methyl valeric acid: K40 (= K47), T69 (= T74), G71 (= G76), T73 (= T78), Q141 (= Q149), G175 (= G183), T176 (= T184), G219 (= G233)
binding pyridoxal-5'-phosphate: K40 (= K47), N72 (= N77), Y172 (≠ C180), G175 (= G183), T176 (= T184), T179 (= T187), G219 (= G233), S263 (= S277), P289 (≠ C303), D290 (= D304)

P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
40% identity, 90% coverage: 14:312/332 of query aligns to 8:289/303 of P16703

query
sites
P16703

I

I

G

G

N

N

T

T

P

P

L

L

V

V

R

K

L

L

K

Q

G

R

P

M

S

G

E

P

A

D

T

N

G

G

C

S

E

E

I

V

L

W

A

L

K

K

C

L

E

E

F

G

M

N

N

N

P

P

G

A

G

G

S

S

V

V

K

K

D

D

R

R

A

A

L

L

A

S

I

M

I

I

T

V

D

E

A

A

E

E

E

K

R

R

G

G

L

E

I

I

A

K

P

P

G

G

G

D

I

V

I

L

V

I

E

E

G

A

T

T

A

S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

L

M

V

I

G

A

N

A

A

L

R

K

G

G

Y

Y

R

R

T

M

I

K

I

L

V

L

M

M

T

P

D

D

T

N

Q

M

S

S

Q

Q

E

E

K

R

Q

R

D

A

T

A

L

M

R

R

A

A

L

Y

G

G

A

A

E

E

L

L

V

I

L

L

V

V

P

T

P

K

T

E

A

Q

Y

G

S

M

N

E

P

G

A

A

H

R

Y

D

V

L

H

-

T

-

S

A

R

L

R

E

I

M

A

A

E

N

E

R

T

G

P

E

G

G

A

K

L

L

W

L

A

-

N

D

Q

Q

F

F

D

N

N

N

T

P

A

D

N

N

R

P

L

Y

A

A

H

H

I

Y

R

T

T

T

A

G

P

P

E

E

I

I

W

W

A

Q

Q

Q

T

T

G

G

R

R

I

I

D

T

G

H

F

F

T

V

C

S

A

S

V

M

G

G

T

T

G

T

G

G

T

T

L

I

A

T

G

G

V

V

G

S

L

R

G

F

L

M

K

R

A

E

F

Q

S

S

E

K

D

P

V

V

V

T

I

I

G

V

L

G

T

L

D

Q

P

P

Y

-

G

-

A

-

L

-

F

-

N

-

Y

-

F

-

A

-

H

-

G

-

E

-

L

-

K

-

A

E

E

E

G

G

S

S

V

I

A

P

E

-

G

G

I

I

G

R

Q

R

-

W

-

P

-

T

S

E

R

Y

I

L

T

P

A

G

N

I

L

F

D

N

G

A

A

S

P

L

V

V

D

D

T

E

Q

V

F

L

R

D

V

I

S

H

D

Q

E

R

E

D

G

A

L

E

E

N

Q

T

V

M

I

R

A

E

L

L

L

A

G

V

S

R

E

E

G

G

L

I

C

F

V

C

G

G

L

V

S
|
S

S

S

G

G

I

G

N

A

V

V

A

A

G

G

A

A

I

L

A

R

L

V

A

A

K

K

E

-

L

A

G

N

P

P

G

D

K

A

T

V

I

V

V

V

T

A

I

I

L

I

C

C

D

D

S

R

G

G

M

D

R

R

Y

Y

L

L

S

S

S

T

N71 (= N77) binding pyridoxal 5'-phosphate
S255 (= S277) binding pyridoxal 5'-phosphate

P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 96% coverage: 6:324/332 of query aligns to 3:316/464 of P9WP51

query
sites
P9WP51

I

I

A

A

P

Q

D

H

A

I

L

S

A

E

L

L

I

I

G

G

N

G

T

T

P

P

L

L

V

V

R

R

L

L

K

N

G

S

P

V

S

V

E

P

A

D

T

G

G

A

C

G

E

T

I

V

L

A

A

A

K

K

C

V

E

E

F

Y

M

L

N

N

P

P

G

G

S

S

V

S

K

K

D

D

R

R

A

I

A

A

L

V

A

K

I

M

I

I

T

E

D

A

A

A

E

E

E

A

R

S

G

G

L

Q

I

L

A

K

P

P

G

G

I

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

G

A

N

Q

A

R

R

R

G

G

Y

Y

R

K

T

C

I

V

I

F

V

V

M

C

T

P

D

D

T

K

Q

V

S

S

Q

E

E

D

K

K

Q

R

D

N

T

V

L

L

R

I

A

A

L

Y

G

G

A

A

E

E

L

V

V

V

L

V

-

C

-

P

-

T

-

A

V

V

P

P

T

-

A

-

Y

-

S

H

N

D

P

P

A

A

H

S

Y

Y

V

Y

H

S

T

V

S

S

R

D

R

R

I

L

A

V

E

R

E

D

T

I

P

D

G

G

A

A

L

W

W

K

A

P

N

D

Q

Q

F

Y

D

A

N

N

T

P

A

E

N

G

R

P

L

A

A

S

H

H

I

Y

R

V

T

T

A

G

P

P

E

E

I

I

W

W

A

A

Q

D

T

T

G

E

G

G

R

K

I

V

D

T

G

H

F

F

T

V

C

A

A

G

V

I

G

G

T

T

G

G

T

T

L

I

A

T

G

G

V

A

G

G

L

R

G

Y

L

L

K

K

A

E

F

V

S

S

-

G

E

G

D

R

V

V

V

R

I

I

G

V

L

G

T

A

D

D

P

P

Y

E

G

G

A

S

A

V

L

-

F

-

N

-

Y

-

F

Y

A

S

H

G

G

G

E

-

L

-

K

-

A

A

E

G

G

R

S

P

S

Y

V

L

A

V

E

E

G

G

I

V

G

G

Q

E

S

D

R

F

I

W

T

P

A

A

N

A

L

Y

D

D

G

P

A

S

P

V

V

P

D

D

T

E

Q

I

F

I

R

A

V

V

S

S

D

D

E

S

E

D

G

S

L

F

E

D

Q

M

V

T

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

A

L

M

C

L

V

V

G

G

L

G

S

S

S

C

G

G

I

M

N

A

V

V

A

V

G

A

A

A

I

L

A

K

L

V

A

A

K

E

E

E

L

A

G

G

P

P

G

D

K

A

T

L

I

I

V

V

T

V

I

L

L

L

C

P

D

D

S

G

G

G

M

R

R

G

Y

Y

L

M

S

S

S

K

L

I

F

F

N

N

P

D

A

A

W

W

L

M

E

S

A

S

K

Y

G

G

L

F

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, 94% coverage: 13:324/332 of query aligns to 8:314/458 of 7xoyA

query
sites
7xoyA

L

L

I

I

G

G

N

G

T

T

P

P

L

L

V

V

R

R

L

L

K

N

G

S

P

V

S

V

E

P

A

D

T

G

G

A

C

G

E

T

I

V

L

A

A

A

K

K

C

V

E

E

F

Y

M

L

N

N

P

P

G

G

S

S

V

S

K
|
K

D

D

R

R

A

I

A

A

L

V

A

K

I

M

I

I

T

E

D

A

A

A

E

E

E

A

R

S

G

G

L

Q

I

L

A

K

P

P

G

G

I

T

I

I

V

V

E

E

G

P

T

T

A
x
S

G

G

N
|
N

T
|
T

G

G

I

V

G

G

L

L

A

A

L

L

V

V

G

A

N

Q

A

R

R

R

G

G

Y

Y

R

K

T

C

I

V

I

F

V

V

M

C

T

P

D

D

T

K

Q

V

S

S

Q

E

E

D

K

K

Q

R

D

N

T

V

L

L

R

I

A

A

L

Y

G

G

A

A

E

E

L

V

V

V

L

V

-

C

-

P

-

T

-

A

V

V

P

P

T

-

A

-

Y

-

S

H

N

D

P

P

A

A

H

S

Y

Y

V

Y

H

S

T

V

S

S

R

D

R

R

I

L

A

V

E

R

E

D

T

I

P

D

G

G

A

A

L

W

W

K

A

P

N

D

Q

Q

F

Y

D

A

N

N

T

P

A

E

N

G

R

P

L

A

A

S

H

H

I

Y

R

V

T

T

A

G

P

P

E

E

I

I

W

W

A

A

Q

D

T

T

G

E

G

G

R

K

I

V

D

T

G

H

F

F

T

V

C

A

A

G

V

I

G

G

T
|
T

G

G

G
|
G

T
|
T

L

I

A

T

G

G

V

A

G

G

L

R

G

Y

L

L

K

K

A

E

F

V

S

S

-

G

E

G

D

R

V

V

V

R

I

I

G

V

L

G

T

A

D

D

P

P

Y

E

G

G

A

S

A

V

L

-

F

-

N

-

Y

-

F

Y

A

S

H

G

G

G

E

-

L

-

K

-

A

A

E

G

G

R

S

P

S

Y

V

L

A

V

E

E

G

G

I

V

G

G

Q

E

S

D

R

F

I

W

T

P

A

A

N

A

L

Y

D

D

G

P

A

S

P

V

V

P

D

D

T

E

Q

I

F

I

R

A

V

V

S

S

D

D

E

S

E

D

G

S

L

F

E

D

Q

M

V

T

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

A

L

M

C

L

V

V

G

G

L

G

S
|
S

S

C

G

G

I

M

N

A

V

V

A

V

G

A

A

A

I

L

A

K

L

V

A

A

K

E

E

E

L

A

G

G

P

P

G

D

K

A

T

L

I

I

V

V

T

V

I

L

L

L

C
x
P

D

D

S

G

G

G

M

R

R

G

Y

Y

L

M

S

S

S

K

L

I

F

F

N

N

P

D

A

A

W

W

L

M

E

S

A

S

K

Y

G

G

L

F

binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: K42 (= K47), S70 (≠ A75), N72 (= N77), T73 (= T78), T180 (= T184), G182 (= G186), T183 (= T187), S267 (= S277), P293 (≠ C303)

7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
40% identity, 94% coverage: 13:324/332 of query aligns to 8:314/458 of 7xnzB

query
sites
7xnzB

L

L

I

I

G

G

N

G

T

T

P

P

L

L

V

V

R

R

L

L

K

N

G

S

P

V

S

V

E

P

A

D

T

G

G

A

C

G

E

T

I

V

L

A

A

A

K

K

C

V

E

E

F

Y

M

L

N

N

P

P

G

G

S

S

V

S

K
|
K

D

D

R

R

A

I

A

A

L

V

A

K

I

M

I

I

T

E

D

A

A

A

E

E

E

A

R

S

G

G

L

Q

I

L

A

K

P

P

G

G

I

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

G

A

N

Q

A

R

R

R

G

G

Y

Y

R

K

T

C

I

V

I

F

V

V

M

C

T

P

D

D

T

K

Q

V

S

S

Q

E

E

D

K

K

Q

R

D

N

T

V

L

L

R

I

A

A

L

Y

G

G

A

A

E

E

L

V

V

V

L

V

-

C

-

P

-

T

-

A

V

V

P

P

T

-

A

-

Y

-

S

H

N

D

P

P

A

A

H

S

Y

Y

V

Y

H

S

T

V

S

S

R

D

R

R

I

L

A

V

E

R

E

D

T

I

P

D

G

G

A

A

L

W

W

K

A

P

N

D

Q

Q

F

Y

D

A

N

N

T

P

A

E

N

G

R

P

L

A

A

S

H

H

I

Y

R

V

T

T

A

G

P

P

E

E

I

I

W

W

A

A

Q

D

T

T

G

E

G

G

R

K

I

V

D

T

G

H

F

F

T

V

C

A

A

G

V

I

G
|
G

T
|
T

G
|
G

T
|
T

L

I

A

T

G

G

V

A

G

G

L

R

G

Y

L

L

K

K

A

E

F

V

S

S

-

G

E

G

D

R

V

V

V

R

I

I

G

V

L

G

T

A

D

D

P

P

Y

E

G

G

A

S

A

V

L

-

F

-

N

-

Y

-

F

Y

A

S

H

G

G

G

E

-

L

-

K

-

A

A

E

G

G

R

S

P

S

Y

V

L

A

V

E

E

G

G

I

V

G

G

Q

E

S

D

R

F

I

W

T

P

A

A

N

A

L

Y

D

D

G

P

A

S

P

V

V

P

D

D

T

E

Q

I

F

I

R

A

V

V

S

S

D

D

E

S

E

D

G

S

L

F

E

D

Q

M

V

T

I

R

A

R

L

L

L

A

G

R

S

E

E

E

G

A

L

M

C

L

V

V

G

G

L

G

S
|
S

S

C

G

G

I

M

N

A

V

V

A

V

G

A

A

A

I

L

A

K

L

V

A

A

K

E

E

E

L

A

G

G

P

P

G

D

K

A

T

L

I

I

V

V

T

V

I

L

L

L

C
x
P

D
|
D

S

G

G

G

M

R

R

G

Y

Y

L

M

S

S

S

K

L

I

F

F

N

N

P

D

A

A

W

W

L

M

E

S

A

S

K

Y

G

G

L

F

binding pyridoxal-5'-phosphate: K42 (= K47), G179 (= G183), T180 (= T184), G181 (= G185), G182 (= G186), T183 (= T187), S267 (= S277), P293 (≠ C303), D294 (= D304)

2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
40% identity, 90% coverage: 14:312/332 of query aligns to 8:289/294 of 2bhtA

query
sites
2bhtA

I

I

G

G

N

N

T

T

P

P

L

L

V

V

R

K

L

L

K

Q

G

R

P

M

S

G

E

P

A

D

T

N

G

G

C

S

E

E

I

V

L

W

A

L

K

K

C

L

E

E

F

G

M

N

N

N

P

P

G

A

G

G

S

S

V

V

K
|
K

D

D

R

R

A

A

L

L

A

S

I

M

I

I

T

V

D

E

A

A

E

E

E

K

R

R

G

G

L

R

I

I

A

K

P

P

G

G

G

D

I

V

I

L

V

I

E

E

G

A

T

T

A
x
S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

L

M

V

I

G

A

N

A

A

L

R

K

G

G

Y

Y

R

R

T

M

I

K

I

L

V

L

M

M

T

P

D

D

T

N

Q

M

S

S

Q

Q

E

E

K

R

Q

R

D

A

T

A

L

M

R

R

A

A

L

Y

G

G

A

A

E

E

L

L

V

I

L

L

V

V

P

T

P

K

T

E

A

Q

Y

G

S

M

N

E

P

G

A

A

H

R

Y

D

V

L

H

-

T

-

S

A

R

L

R

E

I

M

A

A

E

N

E

R

T

G

P

E

G

G

A

K

L

L

W

L

A

-

N

D

Q

Q

F

F

D

N

N

N

T

P

A

D

N

N

R

P

L

K

A

A

H

H

I

Y

R

T

T

T

A

G

P

P

E

E

I

I

W

W

A

Q

Q

Q

T

T

G

G

R

R

I

I

D

T

G

H

F

F

T

V

C

S

A

S

V
x
M

G
|
G

T
|
T

G
x
T

G

G

T
|
T

L

I

A

T

G

G

V

V

G

S

L

E

G

F

L

M

K

R

A

E

F

Q

S

S

E

K

D

P

V

V

V

T

I

I

G

V

L

G

T

L

D
x
Q

P

P

Y

-

G

-

A

-

L

-

F

-

N

-

Y

-

F

-

A

-

H

-

G

-

E

-

L

-

K

-

A

E

E

E

G
|
G

S

S

V

I

A

P

E

-

G
|
G

I

I

G

R

Q

R

-

W

-

P

-

T

S

E

R

Y

I

L

T

P

A

G

N

I

L

F

D

N

G

A

A

S

P

L

V

V

D

D

T

E

Q

V

F

L

R

D

V

I

S

H

D

Q

E

R

E

D

G

A

L

E

E

N

Q

T

V

M

I

R

A

E

L

L

L

A

G

V

S

R

E

E

G

G

L

I

C

F

V

C

G

G

L

V

S
|
S

S

S

G

G

I

G

N

A

V

V

A

A

G

G

A

A

I

L

A

R

L

V

A

A

K

K

E

A

L

-

G

N

P

P

G

D

K

A

T

V

I

V

V

V

T

A

I

I

L

I

C
|
C

D

D

S

R

G

G

M

D

R

R

Y

Y

L

L

S

S

S

T

active site: K41 (= K47), S69 (≠ A75), Q199 (≠ D208), G203 (= G227), S255 (= S277), C280 (= C303)
binding pyridoxal-5'-phosphate: K41 (= K47), N71 (= N77), M173 (≠ V182), G174 (= G183), T175 (= T184), T176 (≠ G185), T178 (= T187), G208 (= G233), S255 (= S277), C280 (= C303)

Query Sequence

>WP_012050142.1 NCBI__GCF_000016765.1:WP_012050142.1
MAHDMIAPDALALIGNTPLVRLKGPSEATGCEILAKCEFMNPGGSVKDRAALAIITDAEE
RGLIAPGGIIVEGTAGNTGIGLALVGNARGYRTIIVMTDTQSQEKQDTLRALGAELVLVP
PTAYSNPAHYVHTSRRIAEETPGALWANQFDNTANRLAHIRTTAPEIWAQTGGRIDGFTC
AVGTGGTLAGVGLGLKAFSEDVVIGLTDPYGAALFNYFAHGELKAEGSSVAEGIGQSRIT
ANLDGAPVDTQFRVSDEEGLEQVIALLGSEGLCVGLSSGINVAGAIALAKELGPGKTIVT
ILCDSGMRYLSSLFNPAWLEAKGLPVPALLRR

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