SitesBLAST

A6QDA0 N-(2-amino-2-carboxyethyl)-L-glutamate synthase; ACEGA synthase; Staphyloferrin B biosynthesis protein SbnA; EC 2.5.1.140 from Staphylococcus aureus (strain Newman) (see paper)
38% identity, 89% coverage: 22:303/317 of query aligns to 33:315/326 of A6QDA0

query
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A6QDA0

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K47 (= K36) modified: N6-(pyridoxal phosphate)lysine
N77 (= N66) binding
R132 (= R121) mutation to A: No detectable enzyme activity. Does not form pyridoxal 5'-phosphate-alpha-aminoacrylate reaction intermediate.
Y152 (= Y141) mutation to F: Very low enzyme activity. Does not form pyridoxal 5'-phosphate-alpha-aminoacrylate reaction intermediate; when associated with G-185.
STTGS 185:189 (≠ GTTGT 173:177) binding
S272 (= S260) binding

5d84A Staphyloferrin b precursor biosynthetic enzyme sbna bound to plp (see paper)
38% identity, 89% coverage: 22:303/317 of query aligns to 27:309/318 of 5d84A

query
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5d84A

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active site: K41 (= K36), S266 (= S260)
binding pyridoxal-5'-phosphate: K41 (= K36), N71 (= N66), V178 (≠ A172), S179 (≠ G173), T180 (= T174), T181 (= T175), S183 (≠ T177), G222 (= G216), S266 (= S260), P292 (= P286), D293 (= D287)

5d86A Staphyloferrin b precursor biosynthetic enzyme sbna y152f variant (see paper)
37% identity, 89% coverage: 22:303/317 of query aligns to 26:308/318 of 5d86A

query
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active site: K40 (= K36), S265 (= S260)
binding magnesium ion: S225 (= S220), R226 (= R221)
binding pyridoxal-5'-phosphate: K40 (= K36), N70 (= N66), V177 (≠ A172), S178 (≠ G173), T179 (= T174), T180 (= T175), S182 (≠ T177), G221 (= G216), S265 (= S260), P291 (= P286), D292 (= D287)

8if7A Crystal structure of cmnb (see paper)
36% identity, 88% coverage: 22:301/317 of query aligns to 38:317/342 of 8if7A

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binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K52 (= K36), T78 (≠ S63), S79 (= S64), N81 (= N66), L82 (= L67), V188 (≠ A172), S189 (≠ G173), T190 (= T174), G191 (≠ T175), T193 (= T177), G232 (= G216), S276 (= S260), A302 (≠ P286), D303 (= D287)

4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
34% identity, 87% coverage: 25:301/317 of query aligns to 66:346/486 of 4pcuA

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4pcuA

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E

E

V

I

I

V

V

R

C

T

D

P

T

A

R

R

-

F

D

D

R

S

N

P

G

S

F

H

L

V

G

G

A

V

R

A

I

W

T

R

L

L

I

K

Q

N

E

E

M

I

I

-

R

-

Q

-

D

-

P

P

R

N

Y

S

F

H

W

I

T

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

A

S

N

N

P
|
P

L
|
L

A

A

H

H

Y
|
Y

N

D

R

T

T

T

A

A

P

D

E

E

I

I

L

L

Q

Q

-

C

H

D

P

G

N

K

C

L

K

D

W

M

L

L

F

V

V

A

G

S

A

V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

I

A

A

R
|
R

Y

K

L

L

R

K

E

E

K

K

A

C

P

P

E

G

V

C

K

R

L

I

I

I

A

G

V

V

D
|
D

T

P

V

E

G

G

S

S

I

I

-

L

-

A

N

E

F

P

Q

E

E

E

V

L

P

N

K

Q

K

T

R

E

L

Q

-

T

-

Y

-

E

I

V

P

E

G
|
G

L

I

G

G

T

Y

S

D

R

F

R

I

P

P

E
x
T

I

V

L

L

E

D

R

R

D

T

L

V

V

V

E

D

H

K

I

W

E

F

F

K

V

S

D

N

E

D

V

E

E

E

T

A

I

F

R

T

M

F

C

A

R

R

S

M

V

L

A

I

Q

A

D

Q

Y

E

G

G

L

L

L

C

G

G

S
|
S

T

A

G

G

T

S

V

T

L

V

V

A

A

V

V

A

K

V

R

K

L

A

R

A

K

Q

Q

E

I

L

P

Q

A

E

G

G

D

Q

E

R

V

C

V

V

I

I

S

L

P
|
P

D
|
D

M

S

G

V

E

R

R

N

Y

Y

L

M

E

T

T

K

I

F

Y

L

S

S

D

D

K

R

W

W

active site: K77 (= K36), S105 (= S64), D237 (= D198), S305 (= S260)
binding protoporphyrin ix containing fe: A182 (≠ P144), P185 (= P147), L186 (= L148), Y189 (= Y151), R222 (= R183), T269 (≠ E224)
binding pyridoxal-5'-phosphate: K77 (= K36), N107 (= N66), G212 (= G173), T213 (= T174), G214 (≠ T175), T216 (= T177), G261 (= G216), S305 (= S260), P331 (= P286), D332 (= D287)

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

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
33% identity, 87% coverage: 25:301/317 of query aligns to 68:350/500 of 7qgtB

query
sites
7qgtB

K

K

I

C

E

E

G

F

L

F

N

N

P

A

A

G

G

G

S

S

I

V

K
|
K

L

D

K

R

T

I

A

S

I

L

S

R

L

M

I

I

E

E

E

D

S

A

E

E

R

R

L

D

G

G

L

T

L

L

S

K

P

P

G

G

R

D

K

T

V

I

I

I

E

E

S

P

S
x
T

S
|
S

G

G

N
|
N

L
x
T

G

G

V

I

A

G

L

L

S

A

M

L

I

A

C

A

A

A

Q

V

R

R

G

G

Y

Y

P

R

F

C

T

I

C

I

I

V

T

M

D

P

P

E

N

K

V

M

N

S

Q

S

V

E

S

K

V

V

N

D

L

V

M

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

I

V

V

R

C

T

D

P

T

T

R

N

-

A

-

R

-

F

D

D

R

S

N

P

G

E

G

S

F

H

L

V

G

G

A

V

R

A

I

W

T

R

L

L

I

K

Q

N

E

E

M

I

I

-

R

-

Q

-

D

-

P

P

R

N

Y

S

F

H

W

I

T

L

N

D

Q
|
Q

Y

Y

A

R

N

N

P
x
A

A

S

N

N

P
|
P

L
|
L

A

A

H

H

Y
|
Y

N

D

R

T

T

T

A

A

P

D

E

E

I

I

L

L

Q

Q

-

C

H

D

P

G

N

K

C

L

K

D

W

M

L

L

F

V

V

A

G

S

A

V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

I

A

A

R
|
R

Y

K

L

L

R

K

E

E

K

K

A

C

P

P

E

G

V

C

K

R

L

I

I

I

A

G

V

V

D

D

T

P

V

E

G

G

S

S

I

I

-

L

-

A

N

E

F

P

Q

E

E

E

V

L

P

N

K

Q

K

T

R

E

L

Q

-

T

-

Y

-

E

I

V

P

E

G
|
G

L

I

G

G

T

Y

S

D

R

F

R

I

P

P

E

T

I

V

L

L

E

D

R

R

D

T

L

V

V

V

E

D

H

K

I

W

E

F

F

K

V

S

D

N

E

D

V

E

E

E

T

A

I

F

R

T

M

F

C

A

R

R

S

M

V

L

A

I

Q

A

D

Q

Y

E

G

G

L

L

L

C

G

G

S
|
S

T

A

G

G

T

S

V

T

L

V

V

A

A

V

V

A

K

V

R

K

L

A

R

A

K

Q

Q

E

I

L

P

Q

A

E

G

G

D

Q

E

R

V

C

V

V

I

I

S

L

P
|
P

D
|
D

M

S

G

V

E

R

R

N

Y

Y

L

M

E

T

T

K

I

F

Y

L

S

S

D

D

K

R

W

W

binding protoporphyrin ix containing fe: A186 (≠ P144), P189 (= P147), L190 (= L148), Y193 (= Y151), R226 (= R183)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K36), T106 (≠ S63), S107 (= S64), N109 (= N66), T110 (≠ L67), Q182 (= Q140), G216 (= G173), T217 (= T174), G218 (≠ T175), T220 (= T177), G265 (= G216), S309 (= S260), P335 (= P286), D336 (= D287)

Sites not aligning to the query:

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

7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
33% identity, 87% coverage: 25:301/317 of query aligns to 68:350/500 of 7qgtA

query
sites
7qgtA

K

K

I

C

E

E

G

F

L

F

N

N

P

A

A

G

G

G

S

S

I

V

K
|
K

L

D

K

R

T

I

A

S

I

L

S

R

L

M

I

I

E

E

E

D

S

A

E

E

R

R

L

D

G

G

L

T

L

L

S

K

P

P

G

G

R

D

K

T

V

I

I

I

E

E

S

P

S

T

S

S

G

G

N
|
N

L

T

G

G

V

I

A

G

L

L

S

A

M

L

I

A

C

A

A

A

Q

V

R

R

G

G

Y

Y

P

R

F

C

T

I

C

I

I

V

T

M

D

P

P

E

N

K

V

M

N

S

Q

S

V

E

S

K

V

V

N

D

L

V

M

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

I

V

V

R

C

T

D

P

T

T

R

N

-

A

-

R

-

F

D

D

R

S

N

P

G

E

G

S

F

H

L

V

G

G

A

V

R

A

I

W

T

R

L

L

I

K

Q

N

E

E

M

I

I

-

R

-

Q

-

D

-

P

P

R

N

Y

S

F

H

W

I

T

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

A

S

N

N

P
|
P

L
|
L

A

A

H

H

Y
|
Y

N

D

R

T

T

T

A

A

P

D

E

E

I

I

L

L

Q

Q

-

C

H

D

P

G

N

K

C

L

K

D

W

M

L

L

F

V

V

A

G

S

A

V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

I

A

A

R
|
R

Y

K

L

L

R

K

E

E

K

K

A

C

P

P

E

G

V

C

K

R

L

I

I

I

A

G

V

V

D

D

T

P

V

E

G

G

S

S

I

I

-

L

-

A

N

E

F

P

Q

E

E

E

V

L

P

N

K

Q

K

T

R

E

L

Q

-

T

-

Y

-

E

I

V

P

E

G
|
G

L

I

G

G

T

Y

S

D

R

F

R

I

P

P

E

T

I

V

L

L

E

D

R

R

D

T

L

V

V

V

E

D

H

K

I

W

E

F

F

K

V

S

D

N

E

D

V

E

E

E

T

A

I

F

R

T

M

F

C

A

R

R

S

M

V

L

A

I

Q

A

D

Q

Y

E

G

G

L

L

L

C

G

G

S
|
S

T

A

G

G

T

S

V

T

L

V

V

A

A

V

V

A

K

V

R

K

L

A

R

A

K

Q

Q

E

I

L

P

Q

A

E

G

G

D

Q

E

R

V

C

V

V

I

I

S

L

P
|
P

D
|
D

M

S

G

V

E

R

R

N

Y

Y

L

M

E

T

T

K

I

F

Y

L

S

S

D

D

K

R

W

W

binding protoporphyrin ix containing fe: A186 (≠ P144), P189 (= P147), L190 (= L148), Y193 (= Y151), R226 (= R183)
binding pyridoxal-5'-phosphate: K79 (= K36), N109 (= N66), G216 (= G173), T217 (= T174), G218 (≠ T175), T220 (= T177), G265 (= G216), S309 (= S260), P335 (= P286), D336 (= D287)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 11, 12, 13, 14, 18, 23, 24, 25

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)
37% identity, 86% coverage: 22:295/317 of query aligns to 27:289/303 of P16703

query
sites
P16703

V

V

Y

W

L

L

K

K

I

L

E

E

G

G

L

N

N

N

P

P

A

A

G

G

S

S

I

V

K

K

L

D

K

R

T

A

A

A

I

L

S

S

L

M

I

I

E

V

E

E

S

A

E

E

R

K

L

R

G

G

L

E

L

I

S

K

P

P

G

G

R

D

K

V

V

L

I

I

E

E

S

A

S

T

S

S

G

G

N
|
N

L

T

G

G

V

I

A

A

L

L

S

A

M

M

I

I

C

A

A

A

Q

L

R

K

G

G

Y

Y

P

R

F

M

T

K

C

L

I

L

T

M

D

P

P

D

N

N

V

M

N

S

Q

Q

V

E

S

R

V

R

N

A

L

A

M

M

K

R

A

A

Y

Y

G

G

A

A

E

E

V

L

I

I

V

L

C

V

D

-

T

T

R

K

D

E

R

Q

N

-

G

-

G

G

F

M

L

E

G

G

A

A

R

R

I

D

T

L

L

A

I

L

Q

E

E

M

M

A

I

N

R

R

Q

G

D

E

P

G

R

K

Y

L

F

L

W

-

T

-

N

D

Q

Q

Y

F

A

N

N

N

P

P

A

D

N

N

P

P

L

Y

A

A

H

H

Y

Y

N

T

R

T

T

T

A

G

P

P

E

E

I

I

L

W

Q

Q

H

T

P

G

N

G

C

R

K

I

W

T

L

H

F

F

V

V

G

S

A

S

-

M

G

G

T

T

G

G

T

T

L

I

I

T

G

G

C

V

A

S

R

R

Y

F

L

M

R

R

E

E

K

Q

A

S

P

K

E

P

V

V

K

T

L

I

I

V

A

G

V

L

D

Q

T

P

V

E

G

-

S

-

I

-

N

E

F

G

Q

S

E

S

V

I

P

P

K

G

K

I

R

R

L

R

I

W

P

P

G

-

L

-

G

-

T

T

S

E

R

Y

R

L

P

P

E

G

I

I

L

F

E

N

R

A

D

S

L

L

V

V

E

D

H

E

I

V

E

L

F

D

V

I

D

H

E

Q

V

R

E

D

T

A

I

E

R

N

M

T

C

M

R

R

S

E

V

L

A

A

Q

V

D

R

Y

E

G

G

L

I

L

F

L

C

G

G

G

V

S
|
S

T

S

G

G

T

G

V

A

L

V

V

A

A

G

V

A

K

L

R

R

L

V

R

A

K

K

Q

A

I

N

P

P

A

-

G

-

D

D

E

A

V

V

-

A

I

I

S

I

P

C

D

D

M

R

G

G

E

D

R

R

Y

Y

L

L

E

S

T

T

N71 (= N66) binding
S255 (= S260) binding

P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
33% identity, 87% coverage: 25:301/317 of query aligns to 108:390/551 of P35520

query
sites
P35520

K

K

I
x
C

E

E

G

F

L

F

N

N

P
x
A

A

G

G

G

S

S

I

V

K
|
K

L

D

K

R

T

I

A

S

I

L

S
x
R

L
x
M

I

I

E

E

E

D

S

A

E
|
E

R

R

L

D

G

G

L

T

L

L

S

K

P

P

G
|
G

R

D

K

T

V

I

I
|
I

E
|
E

S

P

S

T

S

S

G
|
G

N
|
N

L

T

G

G

V

I

A

G

L
|
L

S
x
A

M

L

I

A

C

A

A

A

Q

V

R

R

G

G

Y

Y

P

R

F
x
C

T

I

C

I

I

V

T

M

D

P

P

E

N

K

V
x
M

N

S

Q

S

V
x
E

S

K

V

V

N

D

L
x
V

M

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

I

V

V

R

C
x
T

D

P

T

T

R

N

-

A

-

R

-

F

D

D

R

S

N

P

G

E

G

S

F

H

L

V

G

G

A

V

R

A

I

W

T

R

L

L

I
x
K

Q

N

E

E

M

I

I

-

R

-

Q

-

D

-

P

P

R

N

Y

S

F

H

W

I

T

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

A

S

N
|
N

P

P

L

L

A
|
A

H

H

Y

Y

N
x
D

R

T

T

T

A

A

P

D

E

E

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W

C109 (≠ I26) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P31) 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 (= K36) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ S42) 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 (≠ L43) to V: in CBSD; loss of activity
E131 (= E48) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G56) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (= I60) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E61) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G65) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N66) binding
L154 (= L71) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (≠ S72) 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 (≠ F82) 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 (≠ V90) 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 (≠ V93) 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 (≠ L97) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ C108) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ I125) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ P144) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N146) 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 (= A149) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ N152) 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 (≠ GTTGT 173:177) binding
T257 (= T174) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ I179) 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 (= R183) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (≠ R186) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ A189) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ V192) 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 (= I195) 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 (= D198) to N: in CBSD; loss of activity
A288 (vs. gap) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (vs. gap) 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 (= G216) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G218) 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 (= V231) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (≠ E232) to V: in CBSD; loss of activity
R336 (= R247) 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 (≠ V249) 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 (= G258) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S260) 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 (≠ V264) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ E280) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D287) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ E290) 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 (≠ T295) to E: in CBSD; severe form; dbSNP:rs121964967

Sites not aligning to the query:

18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
52 binding axial binding residue
58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
69 A → P: in dbSNP:rs17849313
78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
85 G → R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
87 T → N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
101 L → P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
102 K → N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; K → Q: in dbSNP:rs34040148
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

5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
36% identity, 88% coverage: 22:301/317 of query aligns to 60:341/488 of 5ohxA

query
sites
5ohxA

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binding protoporphyrin ix containing fe: P181 (= P144), P184 (= P147), Y188 (= Y151), R221 (= R183)
binding pyridoxal-5'-phosphate: K74 (= K36), N104 (= N66), G209 (= G171), G211 (= G173), T212 (= T174), G213 (≠ T175), G214 (= G176), T215 (= T177), G256 (= G216), S300 (= S260), P326 (= P286), D327 (= D287)

Sites not aligning to the query:

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

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
35% identity, 89% coverage: 22:304/317 of query aligns to 64:351/504 of Q2V0C9

query
sites
Q2V0C9

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K78 (= K36) modified: N6-(pyridoxal phosphate)lysine
N108 (= N66) binding
GTGGT 215:219 (≠ GTTGT 173:177) binding
S307 (= S260) binding

Sites not aligning to the query:

12 binding axial binding residue
23 binding axial binding residue

6ahiB Crystal structure of o-acetylserine dependent cystathionine beta- synthase from helicobacter pylori. (see paper)
33% identity, 86% coverage: 22:293/317 of query aligns to 32:300/306 of 6ahiB

query
sites
6ahiB

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T

G

G

V

I

A

A

L

L

S

A

M

L

I

V

C

A

A

I

Q

K

R

H

G

H

Y

L

P

K

F

T

T

I

C

F

I

V

T

V

D

P

P

E

N

K

V

F

N

S

Q

T

V

E

S
x
K

V

Q

N

Q

L

I

M

M

K

R

A

A

Y

L

G

G

A

A

E

L

V

V

I

I

V

N

C

T

D

P

T

T

R

S

D

E

R

-

N

-

G

-

G

G

F

I

L

S

G

G

A

A

R

-

I

I

T

K

L

K

I

S

Q

K

E

E

M

L

I

A

R

E

Q

S

D

I

P

P

R

D

Y

S

F

Y

W

L

T

P

N

L

Q

Q

Y

F

A

E

N

N

P

P

A

D

N

N

P

P

L

A

A

A

H

Y

Y

Y

N

H

R

T

T

L

A

A

P

P

E

E

I

I

L

V

Q

Q

Q

E

-

L

H

G

P

T

N

N

C

L

K

T

W

S

L

F

F

V

V

A

G

G

A

I

G

G

T

S

T

G

G

G

T

T

L

F

I

A

G

G

C

T

A

A

R

R

Y

Y

L

L

R

K

E

E

K

R

A

I

P

P

E

A

V

I

K

R

L

L

I

I

A

G

V

V

D

E

T

P

V

E

G

G

S

S

I

I

N

L

F

N

Q

G

E

G

V

E

P

P

K

G

K

P

R

H

L

E

I

I

P

E

G

G

L

I

G

G

T

V

S

E

R

F

R

I

P

P

E

P

I

F

L

F

E

E

R

N

D

L

L

D

V

I

E

D

H

G

I

F

E

E

F

T

V

I

D

S

E

D

V

E

E

E

T

G

I

F

R

S

M

Y

C

T

R

R

S

K

V

L

A

A

Q

K

D

K

Y

N

G

G

L

L

L

V

G

G

G

S

S
|
S

T

S

G

G

T

A

V

A

L

F

V

V

A

A

V

A

K

L

R

K

L

E

R

A

K

Q

Q

R

I

L

P

P

A

E

G

G

D

S

E

Q

V

V

V

L

V

T

I

I

S

F

P

P

D

D

M

V

G

A

E

D

R

R

Y

Y

L

L

active site: K46 (= K36), S267 (= S260)
binding methionine: K46 (= K36), T73 (≠ S63), A74 (≠ S64), G75 (= G65), N76 (= N66), T77 (≠ L67), K104 (≠ S94)

P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 88% coverage: 22:299/317 of query aligns to 30:307/310 of P9WP55

query
sites
P9WP55

V

I

Y

V

L

A

K

K

I

L

E

E

G

F

L

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

L

D

K

R

T

I

A

G

I

V

S

A

L

M

I

L

E

Q

E

A

S

A

E

E

R

Q

L

A

G

G

L

L

L

I

S

K

P

P

G

D

R

T

K

I

V

I

I

L

E

E

S

P

S

T

S

S

G

G

N
|
N

L

T

G

G

V

I

A

A

L

L

S

A

M

M

I

V

C

C

A

A

Q

A

R

R

G

G

Y

Y

P

R

F

C

T

V

C

L

I

T

T

M

D

P

P

E

N

T

V

M

N

S

Q

L

V

E

S

R

V

R

N

M

L

L

M

L

K

R

A

A

Y

Y

G

G

A

A

E

E

V

L

I

I

V

L

C

T

D

P

T

G

R

A

D

D

R

-

N

-

G

-

G

G

F

M

L

S

G

G

A

A

R

-

I

I

T

A

L

K

I

A

Q

E

E

E

M

L

I

A

R

K

Q

T

D

D

P

Q

R

R

Y

Y

F

F

W

V

T

P

N

Q

Q

Q

Y

F

A

E

N

N

P

P

A

A

N

N

P

P

L

A

A

I

H

H

Y

R

N

V

R

T

T

T

A

A

P

E

E

E

I

V

L

W

Q

R

Q

D

H

T

P

D

N

G

C

K

K

V

W

D

L

I

F

V

V

V

G

A

-

G

A

V

G
|
G

T
|
T

T
x
G

G
|
G

T
|
T

L

I

I

T

G

G

C

V

A

A

R

Q

Y

V

L

I

R

K

E

E

K

R

A

K

P

P

E

S

V

A

K

R

L

F

I

V

A

A

V

V

D

E

T

P

V

A

G

A

S

S

I

P

N

V

F

L

-

S

-

G

Q

Q

E

K

V

G

P

P

K

H

K

P

R

-

L

-

I

I

P

Q

G

G

L

I

G

G

T

A

S

G

R

F

R

V

P

P

E

P

I

V

L

L

E

D

R

Q

D

D

L

L

V

V

E

D

H

E

I

I

E

I

F

T

V

V

D

G

E

N

V

E

E

D

T

A

I

L

R

N

M

V

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

V

G

G

G

I

S
|
S

T

S

G

G

T

A

V

A

L

T

V

V

A

A

V

A

K

L

R

Q

L

V

-

A

R

R

K

R

Q

P

I

E

P

N

A

A

G

G

D

K

E

L

V

I

V

V

I

V

S

L

P

P

D

D

M

F

G

G

E

E

R

R

Y

Y

L

L

E

S

T

T

-

P

I

L

Y

F

S

A

D

D

K44 (= K36) modified: N6-(pyridoxal phosphate)lysine
N74 (= N66) binding
GTGGT 178:182 (≠ GTTGT 173:177) binding
S266 (= S260) binding

2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
35% identity, 86% coverage: 22:295/317 of query aligns to 30:302/306 of 2q3dA

query
sites
2q3dA

V

I

Y

V

L

A

K

K

I

L

E

E

G

F

L

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

L

D

K

R

T

I

A

G

I

V

S

A

L

M

I

L

E

Q

E

A

S

A

E

E

R

Q

L

A

G

G

L

L

L

I

S

K

P

P

G

D

R

T

K

I

V

I

I

L

E

E

S

P

S
x
T

S
|
S

G

G

N
|
N

L
x
T

G

G

V

I

A

A

L

L

S

A

M

M

I

V

C

C

A

A

Q

A

R

R

G

G

Y

Y

P

R

F

C

T

V

C

L

I

T

T

M

D

P

P

E

N

T

V

M

N

S

Q

L

V

E

S

R

V

R

N

M

L

L

M

L

K

R

A

A

Y

Y

G

G

A

A

E

E

V

L

I

I

V

L

C

T

D

P

T

G

R

A

D

D

R

-

N

-

G

-

G

G

F

M

L

S

G

G

A

A

R

-

I

I

T

A

L

K

I

A

Q

E

E

E

M

L

I

A

R

K

Q

T

D

D

P

Q

R

R

Y

Y

F

F

W

V

T

P

N

Q

Q
|
Q

Y

F

A

E

N

N

P

P

A

A

N

N

P

P

L

A

A

I

H

H

Y

R

N

V

R

T

T

T

A

A

P

E

E

E

I

V

L

W

Q

R

Q

D

H

T

P

D

N

G

C

K

K

V

W

D

L

I

F

V

V

V

G

A

-

G

A
x
V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

V

A

A

R

Q

Y

V

L

I

R

K

E

E

K

R

A

K

P

P

E

S

V

A

K

R

L

F

I

V

A

A

V

V

D

E

T

P

V

A

G

A

S

S

I

P

N

V

F

L

-

S

-

G

Q

Q

E

K

V

G

P

P

K

H

K

P

R

-

L

-

I

I

P

Q

G
|
G

L
x
I

G

G

T

A

S

G

R

F

R

V

P

P

E

P

I

V

L

L

E

D

R

Q

D

D

L

L

V

V

E

D

H

E

I

I

E

I

F

T

V

V

D

G

E

N

V

E

E

D

T

A

I

L

R

N

M

V

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

V

G

G

G

I

S
|
S

T

S

G

G

T

A

V

A

L

T

V

V

A

A

V

A

K

L

R

Q

L

V

-

A

R

R

K

R

Q

P

I

E

P

N

A

A

G

G

D

K

E

L

V

I

V

V

I

V

S

L

P
|
P

D
|
D

M

F

G

G

E

E

R

R

Y

Y

L

L

E

S

T

T

active site: K44 (= K36), S266 (= S260), P293 (= P286)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K36), T71 (≠ S63), S72 (= S64), N74 (= N66), T75 (≠ L67), Q144 (= Q140), V177 (≠ A172), G178 (= G173), T179 (= T174), G180 (≠ T175), T182 (= T177), G222 (= G216), I223 (≠ L217), S266 (= S260), P293 (= P286), D294 (= D287)

Q79FV4 S-sulfocysteine synthase; O-phospho-L-serine-dependent S-sulfocysteine synthase; OPS-dependent S-sulfocysteine synthase; O-phosphoserine sulfhydrylase; EC 2.8.5.1; EC 2.5.1.65 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
32% identity, 89% coverage: 23:303/317 of query aligns to 53:331/372 of Q79FV4

query
sites
Q79FV4

Y

W

L

A

K

K

I

L

E

E

G

G

L

F

N

N

P

P

A

G

G

G

S

-

I

M

K

K

L

D

K

R

T

P

A

A

I

L

S

Y

L

M

I

V

E

E

E

C

S

A

E

R

R

A

L

R

G

G

L

D

L

I

S

A

P

P

G

G

R

A

K

A

V

I

I

V

E

E

S

S

S

T

S

G

G

G

N

T

L

L

G

G

V

L

A

G

L

L

S

A

M

L

I

A

C

G

A

K

Q

V

R

Y

G

R

Y

H

P

P

F

V

T

T

C

L

I

V

T

T

D

D

P

P

N

G

V

L

N

E

Q

P

V

I

S

I

V

A

N

R

L

M

M

L

K

T

A

A

Y

Y

G

G

A

A

E

G

V

V

I

D

V

M

C

V

D

T

T

Q

R

P

D

H

R

P

N

V

G

G

F

W

L

Q

G

Q

A

A

R

R

I

K

T

D

L

R

I

V

Q

A

E

Q

M

L

I

M

R

A

Q

E

D

Y

P

P

R

G

Y

A

F

W

W

N

T

P

N

N

Q

Q

Y

Y

A

G

N

N

P

P

A

D

N

N

P

-

L

V

A

G

H

A

Y

Y

N

R

R

S

T

L

A

A

P

L

E

E

I

L

L

V

Q

A

Q

Q

H

L

P

G

N

R

C

I

K

D

W

V

L

L

F

V

V

C

G

S

A

V

G

G

T

T

T

G

G

G

T

H

L

S

I

A

G

G

C

V

A

A

R

R

Y

V

L

L

R

R

E

E

K

F

A

N

P

P

E

D

V

M

K

R

L

L

I

I

A

G

V

V

D

D

T

T

V

I

G

G

S

S

I

T

N

I

F

F

Q

G

E

Q

V

P

P

A

K

S

K

N

R

R

L

L

I

M

P
x
R

G

G

L

L

G

G

T

S

S

S

R

I

R

Y

P

P

E

R

I

N

L

V

E

D

R

Y

D

R

L

A

V

F

E

D

H

E

I

V

E

H

F

W

V

V

D

A

E

P

V

P

E

E

T

A

I

V

R

W

M

A

C

C

R

R

S

S

V

L

A

A

Q

A

D

T

Y

H

G

Y

L

A

L

S

L

G

G

G

G

W

S

S

T

V

G

G

T

A

V

V

L

A

V

L

A

V

V

A

K

G

R

W

L

A

R

A

K

R

Q

N

I

L

P

P

A

A

G

D

D

T

E

T

V

I

V

A

I

V

S

F

P

P

D

D

M

G

G

P

E

Q

R

R

Y

Y

L

F

E

D

T

T

I

I

Y

Y

S

N

D

D

K

A

W

Y

C

C

D

N

R243 (≠ P215) mutation to A: 10-fold decrease in the specificity constant for thiosulfate compared to wild-type enzyme but little change in the specificity constant for the substrate OPS.

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
35% identity, 86% coverage: 22:293/317 of query aligns to 30:300/300 of 3zeiA

query
sites
3zeiA

V

I

Y

V

L

A

K

K

I

L

E

E

G

F

L

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

L

D

K

R

T

I

A

G

I

V

S

A

L

M

I

L

E

Q

E

A

S

A

E

E

R

Q

L

A

G

G

L

L

L

I

S

K

P

P

G

D

R

T

K

I

V

I

I

L

E

E

S

P

S
x
T

S
|
S

G

G

N
|
N

L

T

G

G

V

I

A

A

L

L

S

A

M

M

I

V

C

C

A

A

Q

A

R

R

G

G

Y

Y

P

R

F

C

T

V

C

L

I

T

T

M

D

P

P

E

N

T

V

M

N

S

Q

L

V

E

S

R

V

R

N

M

L

L

M

L

K

R

A

A

Y

Y

G

G

A

A

E

E

V

L

I

I

V

L

C

T

D

P

T

G

R

A

D

D

R

-

N

-

G

-

G

G

F

M

L

S

G

G

A

A

R

-

I
|
I

T

A

L

K

I

A

Q

E

E

E

M

L

I

A

R

K

Q

T

D

D

P

Q

R

R

Y

Y

F

F

W

V

T

P

N

Q

Q
|
Q

Y
x
F

A

E

N

N

P

P

A

A

N

N

P

P

L

A

A

I

H

H

Y

R

N

V

R

T

T

T

A

A

P

E

E

E

I

V

L

W

Q

R

Q

D

H

T

P

D

N

G

C

K

K

V

W

D

L

I

F

V

V

V

G

A

-

G

A
x
V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

V

A

A

R

Q

Y

V

L

I

R

K

E

E

K

R

A

K

P

P

E

S

V

A

K

R

L

F

I

V

A

A

V

V

D

E

T

P

V

A

G

A

S

S

I

P

N

V

F

L

-

S

-

G

Q

Q

E
x
K

V

G

P

P

K

H

K

P

R

-

L

-

I

I

P

Q

G
|
G

L

I

G

G

T
x
A

S

G

R
x
F

R

V

P

P

E

P

I

V

L

L

E

D

R

Q

D

D

L

L

V

V

E

D

H

E

I

I

E

I

F

T

V

V

D

G

E

N

V

E

E

D

T

A

I

L

R

N

M

V

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

V

G

G

G

I

S
|
S

T

S

G

G

T

A

V

A

L

T

V

V

A

A

V

A

K

L

R

Q

L

V

-

A

R

R

K

R

Q

P

I

E

P

N

A

A

G

G

D

K

E

L

V

I

V

V

I

V

S

L

P
|
P

D
|
D

M

F

G

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K36), S266 (= S260), P293 (= P286)
binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (≠ S63), S72 (= S64), I126 (= I122), Q144 (= Q140), F145 (≠ Y141), K215 (≠ E207), G222 (= G216), A225 (≠ T219), F227 (≠ R221)
binding pyridoxal-5'-phosphate: K44 (= K36), N74 (= N66), V177 (≠ A172), G178 (= G173), T179 (= T174), G180 (≠ T175), T182 (= T177), G222 (= G216), S266 (= S260), P293 (= P286), D294 (= D287)

2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
35% identity, 86% coverage: 22:293/317 of query aligns to 30:300/300 of 2q3cA

query
sites
2q3cA

V

I

Y

V

L

A

K

K

I

L

E

E

G

F

L

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

L

D

K

R

T

I

A

G

I

V

S

A

L

M

I

L

E

Q

E

A

S

A

E

E

R

Q

L

A

G

G

L

L

L

I

S

K

P

P

G

D

R

T

K

I

V

I

I

L

E

E

S

P

S
x
T

S
|
S

G
|
G

N

N

L
x
T

G

G

V

I

A

A

L

L

S

A

M

M

I

V

C

C

A

A

Q

A

R

R

G

G

Y

Y

P

R

F

C

T

V

C

L

I

T

T

M

D

P

P

E

N

T

V

M

N

S

Q

L

V

E

S

R

V

R

N

M

L

L

M

L

K

R

A

A

Y

Y

G

G

A

A

E

E

V

L

I

I

V

L

C

T

D

P

T

G

R

A

D

D

R

-

N

-

G

-

G

G

F
x
M

L

S

G

G

A

A

R

-

I

I

T

A

L

K

I

A

Q

E

E

E

M

L

I

A

R

K

Q

T

D

D

P

Q

R

R

Y

Y

F

F

W

V

T

P

N

Q

Q
|
Q

Y

F

A

E

N

N

P

P

A

A

N

N

P

P

L

A

A

I

H

H

Y

R

N

V

R

T

T

T

A

A

P

E

E

E

I

V

L

W

Q

R

Q

D

H

T

P

D

N

G

C

K

K

V

W

D

L

I

F

V

V

V

G

A

-

G

A

V

G

G

T

T

T

G

G

G

T

T

L

I

I

T

G

G

C

V

A

A

R

Q

Y

V

L

I

R

K

E

E

K

R

A

K

P

P

E

S

V

A

K

R

L

F

I

V

A

A

V

V

D

E

T

P

V

A

G

A

S

S

I

P

N

V

F

L

-

S

-

G

Q

Q

E
x
K

V

G

P

P

K

H

K

P

R

-

L

-

I

I

P

Q

G
|
G

L

I

G

G

T
x
A

S

G

R

F

R

V

P

P

E

P

I

V

L

L

E

D

R

Q

D

D

L

L

V

V

E

D

H

E

I

I

E

I

F

T

V

V

D

G

E

N

V

E

E

D

T

A

I

L

R

N

M

V

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

V

G

G

G

I

S
|
S

T

S

G

G

T

A

V

A

L

T

V

V

A

A

V

A

K

L

R

Q

L

V

-

A

R

R

K

R

Q

P

I

E

P

N

A

A

G

G

D

K

E

L

V

I

V

V

I

V

S

L

P
|
P

D

D

M

F

G

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K36), S266 (= S260), P293 (= P286)
binding : T71 (≠ S63), S72 (= S64), G73 (= G65), T75 (≠ L67), M122 (≠ F117), Q144 (= Q140), K215 (≠ E207), G222 (= G216), A225 (≠ T219)

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
35% identity, 86% coverage: 22:295/317 of query aligns to 26:298/302 of 2efyA

query
sites
2efyA

V

V

Y

W

L

V

K

K

I

L

E

E

G

G

L

L

N

N

P

P

A

G

G

G

S

S

I

I

K
|
K

L

D

K

R

T

P

A

A

I

W

S

Y

L

M

I

I

E

K

E

D

S

A

E

E

R

E

L

R

G

G

L

I

L

L

S

R

P

P

G

G

-

S

-

G

R

Q

K

V

V

I

I

V

E

E

S

P

S
x
T

S
|
S

G
|
G

N
|
N

L
x
T

G

G

V

I

A

G

L

L

S

A

M

M

I

I

C

A

A

A

Q

S

R

R

G

G

Y

Y

P

R

F

L

T

I

C

L

I

T

T

M

D

P

P

A

N

Q

V

M

N

S

Q

E

V

E

S

R

V

K

N

R

L

V

M

L

K

K

A

A

Y

F

G

G

A

A

E

E

V

L

I

V

V

L

C

T

D

D

T

P

R

E

D

R

R

R

N

-

G

-

F

M

L

L

G

A

A

A

R

R

I

E

T

E

L

A

I

L

Q

R

E

-

M

-

I

L

R

K

Q

E

D

E

P

L

R

G

Y

A

F

F

W

M

T

P

N

D

Q
|
Q

Y

F

A

K

N

N

P

P

A

A

N

N

P

V

L

R

A

A

H

H

Y

Y

N

E

R

T

T

T

A

G

P

P

E

E

I

L

L

Y

Q

E

Q

A

H

L

P

E

N

G

C

R

K

I

W

D

L

A

F

F

V

V

-
x
Y

G

G

A

S

G
|
G

T
|
T

T
x
G

G

G

T
|
T

L

I

I

T

G

G

C

V

A

G

R

R

Y

Y

L

L

R

K

E

E

K

R

A

I

P

P

E

H

V

V

K

K

L

V

I

I

A

A

V

V

D
x
E

-

P

-

A

-

R

-
x
S

-

N

-

V

-

L

-

S

-

G

T

K

V

M

G

G

S

Q

I

H

N

G

F

F

Q

Q

E

-

V

-

P

-

K

-

R

-

L

-

I

-

P

-

G
|
G

L
x
M

G

G

T
x
P

S

G

R

F

R

I

P

P

E

E

I

N

L

L

E

D

R

L

D

S

L

L

V

L

E

D

H

G

I

V

E

I

F

Q

V

V

D

W

E

E

V

E

E

D

T

A

I

F

R

P

M

L

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

F

L

L

G

G

G

M

S
|
S

T

S

G

G

T

G

V

I

L

V

V

W

A

A

V

A

K

L

R

Q

L

V

R

A

K

R

Q

E

I

L

P

G

A

P

G

G

D

K

E

R

V

V

V

A

V

C

I

I

S

S

P
|
P

D
|
D

M

G

G

G

E

W

R

K

Y

Y

L

L

E

S

T

T

active site: K40 (= K36), S70 (= S64), E200 (≠ D198), S204 (vs. gap), S263 (= S260)
binding 5-oxohexanoic acid: T69 (≠ S63), G71 (= G65), T73 (≠ L67), Q141 (= Q140), G175 (= G173), G219 (= G216), M220 (≠ L217), P222 (≠ T219)
binding pyridoxal-5'-phosphate: K40 (= K36), N72 (= N66), Y172 (vs. gap), G175 (= G173), T176 (= T174), G177 (≠ T175), T179 (= T177), G219 (= G216), S263 (= S260), P289 (= P286), D290 (= D287)

2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
35% identity, 86% coverage: 22:295/317 of query aligns to 26:298/302 of 2ecqA

query
sites
2ecqA

V

V

Y

W

L

V

K

K

I

L

E

E

G

G

L

L

N

N

P

P

A

G

G

G

S

S

I

I

K
|
K

L

D

K

R

T

P

A

A

I

W

S

Y

L

M

I

I

E

K

E

D

S

A

E

E

R

E

L

R

G

G

L

I

L

L

S

R

P

P

G

G

-

S

-

G

R

Q

K

V

V

I

I

V

E

E

S

P

S

T

S
|
S

G
|
G

N
|
N

L
x
T

G

G

V

I

A

G

L

L

S

A

M

M

I

I

C

A

A

A

Q

S

R

R

G

G

Y

Y

P

R

F

L

T

I

C

L

I

T

T

M

D

P

P

A

N

Q

V

M

N

S

Q

E

V

E

S

R

V

K

N

R

L

V

M

L

K

K

A

A

Y

F

G

G

A

A

E

E

V

L

I

V

V

L

C

T

D

D

T

P

R

E

D

R

R

R

N

-

G

-

F

M

L

L

G

A

A

A

R

R

I

E

T

E

L

A

I

L

Q

R

E

-

M

-

I

L

R

K

Q

E

D

E

P

L

R

G

Y

A

F

F

W

M

T

P

N

D

Q
|
Q

Y

F

A

K

N

N

P

P

A

A

N

N

P

V

L

R

A

A

H

H

Y

Y

N

E

R

T

T

T

A

G

P

P

E

E

I

L

L

Y

Q

E

Q

A

H

L

P

E

N

G

C

R

K

I

W

D

L

A

F

F

V

V

-
x
Y

G
|
G

A

S

G
|
G

T
|
T

T

G

G

G

T
|
T

L

I

I

T

G

G

C

V

A

G

R

R

Y

Y

L

L

R

K

E

E

K

R

A

I

P

P

E

H

V

V

K

K

L

V

I

I

A

A

V

V

D
x
E

-

P

-

A

-

R

-
x
S

-

N

-

V

-

L

-

S

-

G

T

K

V

M

G

G

S

Q

I

H

N

G

F

F

Q

Q

E

-

V

-

P

-

K

-

R

-

L

-

I

-

P

-

G
|
G

L

M

G

G

T

P

S

G

R

F

R

I

P

P

E

E

I

N

L

L

E

D

R

L

D

S

L

L

V

L

E

D

H

G

I

V

E

I

F

Q

V

V

D

W

E

E

V

E

E

D

T

A

I

F

R

P

M

L

C

A

R

R

S

R

V

L

A

A

Q

R

D

E

Y

E

G

G

L

L

L

F

L

L

G

G

G

M

S
|
S

T

S

G

G

T

G

V

I

L

V

V

W

A

A

V

A

K

L

R

Q

L

V

R

A

K

R

Q

E

I

L

P

G

A

P

G

G

D

K

E

R

V

V

V

A

V

C

I

I

S

S

P
|
P

D

D

M

G

G

G

E

W

R

K

Y

Y

L

L

E

S

T

T

active site: K40 (= K36), S70 (= S64), E200 (≠ D198), S204 (vs. gap), S263 (= S260)
binding (3s)-3-hydroxybutanoic acid: K40 (= K36), G71 (= G65), T73 (≠ L67), Q141 (= Q140), G219 (= G216)
binding pyridoxal-5'-phosphate: K40 (= K36), N72 (= N66), Y172 (vs. gap), G173 (= G171), G175 (= G173), T176 (= T174), T179 (= T177), G219 (= G216), S263 (= S260), P289 (= P286)

Query Sequence

>Pf6N2E2_3321 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_3321
MMQIYSANQYHKLANFIGDVPVYLKIEGLNPAGSIKLKTAISLIEESERLGLLSPGRKVI
ESSSGNLGVALSMICAQRGYPFTCITDPNVNQVSVNLMKAYGAEVIVCDTRDRNGGFLGA
RITLIQEMIRQDPRYFWTNQYANPANPLAHYNRTAPEILQQHPNCKWLFVGAGTTGTLIG
CARYLREKAPEVKLIAVDTVGSINFQEVPKKRLIPGLGTSRRPEILERDLVEHIEFVDEV
ETIRMCRSVAQDYGLLLGGSTGTVLVAVKRLRKQIPAGDEVVVISPDMGERYLETIYSDK
WCDANFGSQMYQHAMVG

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