SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_019867406.1 NCBI__GCF_000384075.1:WP_019867406.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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)
66% identity, 98% coverage: 5:294/296 of query aligns to 3:292/303 of P16703

query
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P16703

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N71 (= N73) binding pyridoxal 5'-phosphate
S255 (= S257) binding pyridoxal 5'-phosphate

2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
65% identity, 98% coverage: 5:294/296 of query aligns to 3:292/294 of 2bhtA

query
sites
2bhtA

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active site: K41 (= K43), S69 (= S71), Q199 (= Q201), G203 (≠ N205), S255 (= S257), C280 (= C282)
binding pyridoxal-5'-phosphate: K41 (= K43), N71 (= N73), M173 (= M175), G174 (= G176), T175 (= T177), T176 (= T178), T178 (= T180), G208 (= G210), S255 (= S257), C280 (= C282)

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
45% identity, 96% coverage: 10:294/296 of query aligns to 12:306/310 of 5xoqA

query
sites
5xoqA

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binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), M123 (= M121), Q144 (= Q142), R218 (≠ N205), H219 (≠ S206), Q222 (≠ P209), G223 (= G210), A226 (≠ Q216)

2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
43% identity, 98% coverage: 6:294/296 of query aligns to 7:306/320 of 2isqA

query
sites
2isqA

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active site: K44 (= K43), S267 (= S257)
binding pyridoxal-5'-phosphate: K44 (= K43), N75 (= N73), G177 (≠ S174), G179 (= G176), T180 (= T177), G181 (≠ T178), T183 (= T180), G223 (vs. gap), S267 (= S257), P294 (≠ C282)
binding : T72 (= T70), S73 (= S71), G74 (= G72), T76 (= T74), G122 (≠ S120), M123 (= M121), K124 (≠ E122), G217 (≠ W214), P218 (= P215), H219 (≠ Q216), Q222 (vs. gap), G223 (vs. gap)

P47998 Cysteine synthase 1; At.OAS.5-8; Beta-substituted Ala synthase 1;1; ARAth-Bsas1;1; CSase A; AtCS-A; Cys-3A; O-acetylserine (thiol)-lyase 1; OAS-TL A; O-acetylserine sulfhydrylase; Protein ONSET OF LEAF DEATH 3; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
43% identity, 98% coverage: 6:294/296 of query aligns to 9:308/322 of P47998

query
sites
P47998

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A

G

E

N

G

T

C

S

V

N

G

T

R

I

V

L

A

A

A

K

K

L

L

E

E

G

M

N

M

N

E

P

P

A

C

G

S

S

S

I

V

K
|
K

D

D

R

R

P

I

A

G

L

F

S

S

M

M

I

I

K

S

H

D

A

A

E

E

A

K

R

K

G

G

E

L

I

I

K

K

P

P

G

G

D

E

R

S

-

V

L

L

I

I

E

E

A

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

V

A

G

L

L

A

A

M

F

A

T

A

A

I

A

K

K

G

G

Y

Y

K

K

M

L

T

I

L

I

I

T

M

M

P

P

D

A

N

S

M

M

S

S

E

T

E

E

R

R

A

I

S

I

I

L

K

L

A

A

Y

F

G

G

A

V

E

E

I

L

I

V

L

L

T

T

P

D

A

P

A

A

G

K

S

G

M

M

E

K

A

G

A

A

I

I

D

A

L

K

A

A

R

E

S

E

M

I

E

L

A

A

A

K

G

T

-

P

E

N

G

G

K

Y

I

M

L

L

D

Q

Q
|
Q

F

F

A

E

N

N

P

P

D

A

N

N

P

P

R

K

A

I

H
|
H

Y

Y

E

E

S

T

T

T

G
|
G

P

P

E

E

I

I

W

W

R

K

D

G

T

T

Q

G

G

G

Q

K

I

I

T

D

H

G

F

F

V

V

S

S

S

G

M

I

G
|
G

T
|
T

T
x
G

G
|
G

T
|
T

I

I

M

T

G

G

N

A

S

G

R

K

F

Y

L

L

K

K

E

E

Q

Q

N

N

P

A

N

N

I

V

Q

K

I

L

I

Y

G

G

V

V

Q

E

P

P

E

V

G

E

N

S

S

A

K

I

I

L

P

S

G

G

I

G

R
x
K

R

P

W

G

P

P

Q
x
H

E
x
K

-

I

-

Q

-

G

-

I

-

G

-

A

-

G

Y

F

L

I

P

P

K

S

I

V

Y

L

Q

N

A

V

E

D

R

L

V

I

D

D

R

E

I

V

D

Q

V

V

D

S

Q

S

A

D

T

E

A

S

E

I

E

D

T

M

T

A

R

R

A

Q

L

L

A

A

A

L

R

K

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

A

S

A

V

A

A

A

L

I

K

K

L

L

S

A

A

Q

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

F

V

V

V

A

I

I

V

F

C

P

D

S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

V

V

L

F

F

K46 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
T74 (= T70) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
S75 (= S71) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
N77 (= N73) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
T78 (= T74) mutation T->A,S: Reduction of cysteine synthase activity.
Q147 (= Q142) mutation Q->A,E: Strong reduction of cysteine synthase activity.
H157 (= H152) mutation H->Q,N: Slight reduction of cysteine synthase activity.
G162 (= G157) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (≠ GTTGT 176:180) binding pyridoxal 5'-phosphate
T182 (= T177) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T180) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ R212) mutation to A: Impaired interaction with SAT1.
H221 (≠ Q216) mutation to A: Impaired interaction with SAT1.
K222 (≠ E217) mutation to A: Impaired interaction with SAT1.
S269 (= S257) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.

8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
41% identity, 99% coverage: 2:294/296 of query aligns to 9:311/329 of 8b9wA

query
sites
8b9wA

I

V

Y

A

P

P

T

S

I

V

E

D

S

A

F

L

V

I

G

G

N

N

T

T

P

P

L

A

V

V

R

Y

L

L

Q

R

R

N

L

M

P

-

G

N

N

K

T

T

S

A

N

A

T

T

I

I

L

V

A

L

K

K

L

L

E

E

G

S

N

E

N

N

P

P

A

M

G

A

S

S

I

V

K
|
K

D

D

R

R

P

L

A

A

L

Y

S

A

M

I

I

Y

K

D

H

K

A

A

E

E

A

K

R

E

G

G

E

K

I

I

K

K

P

R

G

G

D

K

R

S

L

V

I

I

-

V

E

E

A

A

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

A

L

L

A

A

M

L

A

L

A

G

A

A

I

V

K

R

G

G

Y

Y

K

K

M

V

T

I

L

I

I

T

M

M

P

P

D

D

N

S

M

M

S

S

E

M

E

E

R

R

A

S

S

L

I

L

K

R

A

I

Y

F

G

G

A

A

E

E

I

L

I

I

L

L

T

T

P

P

A

A

A

S

G

L

S

G

M

M

E

K

A

G

A

A

I

V

D

A

L

M

A

A

R

N

S

R

M

I

E

V

A

S

A

N

G

N

E

P

G

D

K

A

I

V

L

L

-

A

D

D

Q

Q

F

F

A

C

N

T

P

K

D

Y

N

N

P

A

R

Q

A

I

H

H

Y

E

E

E

S

T

T

T

G

G

P

P

E

E

I

I

W

W

R

R

D

Q

T

T

Q

K

G

G

Q

H

I

V

T

D

H

C

F

F

V

V

S

A

S

G

M

V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

I

L

M

T

G

G

N

V

S

A

R

R

F

F

L

L

K

K

E

S

Q

V

N

G

P

C

N

N

I

A

Q

N

I

I

I

V

G

A

V

V

Q

E

P

P

E

Q

G

E

N

S

S

P

K

V

I

L

P

S

G

G

I

G

R

R

R

P

W

G

P

P

Q

H

E

R

-

I

-

Q

-
x
G

-

I

-

G

-

A

-

G

Y

F

L

V

P

P

K

E

I

V

Y

L

Q

D

A

R

E

E

R

L

V

V

D

D

R

E

I

I

D

Q

V

V

D

S

Q

S

A

D

T

K

A

A

E

I

E

E

T

T

T

A

R

Q

A

K

L

L

A

S

A

R

R

M

E

D

G

G

I

I

F

F

A

C

G

G

I

F

S
|
S

S

A

G

G

G

A

A

N

V

V

S

F

V

A

A

A

L

L

K

K

L

I

S

A

A

E

-

R

-

P

E

E

L

M

E

A

N

G

A

K

V

T

I

I

V

V

V

T

I

V

V

I

C
x
P

D

S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

A

V

L

F

Y

binding pyridoxal-5'-phosphate: K49 (= K43), N80 (= N73), G184 (= G176), T185 (= T177), G186 (≠ T178), T188 (= T180), G228 (vs. gap), S272 (= S257), P299 (≠ C282)

1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
43% identity, 98% coverage: 6:294/296 of query aligns to 7:306/320 of 1z7yA

query
sites
1z7yA

I

V

E

T

S

E

F

L

V

I

G

G

N

N

T

T

P

P

L

L

V

V

R

Y

L

L

Q

N

R

N

L

V

P

A

G

E

N

G

T

C

S

V

N

G

T

R

I

V

L

A

A

A

K

K

L

L

E

E

G

M

N

M

N

E

P

P

A

C

G

S

S

S

I

V

K
x
A

D

D

R

R

P

I

A

G

L

F

S

S

M

M

I

I

K

S

H

D

A

A

E

E

A

K

R

K

G

G

E

L

I

I

K

K

P

P

G

G

D

E

R

S

-

V

L

L

I

I

E

E

A

P

T

T

S

S

G
|
G

N
|
N

T
|
T

G

G

I

V

A

G

L

L

A

A

M

F

A

T

A

A

I

A

K

K

G

G

Y

Y

K

K

M

L

T

I

L

I

I

T

M

M

P

P

D

A

N

S

M

M

S

S

E

T

E

E

R

R

A

I

S

I

I

L

K

L

A

A

Y

F

G

G

A

V

E

E

I

L

I

V

L

L

T

T

P

D

A

P

A

A

G

K

S

G

M

M

E

K

A

G

A

A

I

I

D

A

L

K

A

A

R

E

S

E

M

I

E

L

A

A

A

K

G

T

-

P

E

N

G

G

K

Y

I

M

L

L

D

Q

Q
|
Q

F

F

A

E

N

N

P

P

D

A

N

N

P

P

R

K

A

I

H

H

Y

Y

E

E

S

T

T

T

G

G

P

P

E

E

I

I

W

W

R

K

D

G

T

T

Q

G

G

G

Q

K

I

I

T

D

H

G

F

F

V

V

S

S

S

G

M
x
I

G
|
G

T
|
T

T
x
G

G

G

T
|
T

I

I

M

T

G

G

N

A

S

G

R

K

F

Y

L

L

K

K

E

E

Q

Q

N

N

P

A

N

N

I

V

Q

K

I

L

I

Y

G

G

V

V

Q

E

P

P

E

V

G

E

N

S

S

A

K

I

I

L

P

S

G

G

I

G

R

K

R

P

W

G

P

P

Q

H

E

K

-

I

-

Q

-
x
G

-

I

-

G

-

A

-

G

Y

F

L

I

P

P

K

S

I

V

Y

L

Q

N

A

V

E

D

R

L

V

I

D

D

R

E

I

V

D

Q

V

V

D

S

Q

S

A

D

T

E

A

S

E

I

E

D

T

M

T

A

R

R

A

Q

L

L

A

A

A

L

R

K

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

A

S

A

V

A

A

A

L

I

K

K

L

L

S

A

A

Q

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

F

V

V

V

A

I

I

V

F

C
x
P

D
x
S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

V

V

L

F

F

active site: A44 (≠ K43), S267 (= S257)
binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G72), N75 (= N73), T76 (= T74), Q145 (= Q142), I178 (≠ M175), G179 (= G176), T180 (= T177), G181 (≠ T178), T183 (= T180), G223 (vs. gap), S267 (= S257), P294 (≠ C282), S295 (≠ D283)

7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
43% identity, 98% coverage: 6:294/296 of query aligns to 7:306/309 of 7n2tA

query
sites
7n2tA

I

V

E

T

S

E

F

L

V

I

G

G

N

N

T

T

P

P

L

L

V

V

R

Y

L

L

Q

N

R

R

L

V

P

V

G

D

N

G

T

C

S

V

N

A

T

R

I

V

L

A

A

A

K

K

L

L

E

E

G

M

N

M

N

E

P

P

A

C

G

S

S

S

I

V

K

K

D

D

R

R

P

I

A

G

L

Y

S

S

M

M

I

I

K

S

H

D

A

A

E

E

A

N

R

K

G

G

E

L

I

I

K

T

P

P

G

G

D

E

R

S

-

V

L

L

I

I

E

E

A

P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

G

L

L

A

A

M

F

A

I

A

A

I

A

K

K

G

G

Y

Y

K

R

M

L

T

I

L

I

I

C

M

M

P

P

D

A

N

S

M

M

S

S

E

L

E

E

R

R

A

T

S

I

I

L

K

R

A

A

Y

F

G

G

A

A

E

E

I

L

I

V

L

L

T

T

P

D

A

P

A

A

G

R

S

G

M

M

E

K

A

G

A

A

I

V

D

Q

L

K

A

A

R

E

S

E

M

I

E

K

A

A

A

K

G

T

-

P

E

N

G

S

K

Y

I

I

L

L

D

Q

Q

Q

F

F

A

E

N

N

P

P

D

A

N

N

P

P

R

K

A

I

H

H

Y

Y

E

E

S

T

T

T

G

G

P

P

E

E

I

I

W

W

R

R

D

G

T

S

Q

G

G

G

Q

K

I

I

T

D

H

A

F

L

V

V

S

S

S

G

M

I

G

G

T

T

T

G

G

G

T

T

I

V

M

T

G

G

N

A

S

G

R

K

F

Y

L

L

K

K

E

E

Q

Q

N

N

P

P

N

N

I

I

Q

K

I

L

I

Y

G

G

V

V

Q

E

P

P

E

V

G

E

N

S

S

A

K

I

I

L

P

S

G

G

I

G

R

K

R

P

W

G

P

P

Q

H

E

K

-

I

-

Q

-

G

-

I

-

G

-

A

-

G

Y

F

L

I

P

P

K

G

I

V

Y

L

Q

D

A

V

E

N

R

L

V

L

D

D

R

E

I

V

I

I

D

Q

V

V

D

S

Q

S

A

E

T

E

A

S

E

I

E

E

T

T

T

A

R

K

A

L

L

L

A

A

A

L

R

K

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S

S

G

G

G

A

A

A

V

A

S

A

V

A

A

A

L

I

K
x
R

L

I

S

A

A

K

E
x
R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

I

V

V

V

A

I

V

V

F

C

P

D

S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

V

V

L

F

F

binding phosphate ion: R277 (≠ K267), R281 (≠ E271)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
42% identity, 99% coverage: 2:294/296 of query aligns to 13:316/323 of 4aecA

query
sites
4aecA

I

I

Y

A

P

D

T

N

I

V

E

S

S

Q

F

L

V

I

G

G

N

K

T

T

P

P

L

M

V

V

R

Y

L

L

Q

N

R

S

L

I

P

A

G

K

N

G

T

C

S

V

N

A

T

N

I

I

L

A

A

A

K

K

L

L

E

E

G

I

N

M

N

E

P

P

A

C

G

C

S

S

I

V

K
|
K

D

D

R

R

P

I

A

G

L

Y

S

S

M

M

I

V

K

T

H

D

A

A

E

E

A

Q

R

K

G

G

E

F

I

I

K

S

P

P

G

G

D

K

R

S

-

V

L

L

I

V

E

E

A

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

G

L

L

A

A

M

F

A

I

A

A

I

S

K

R

G

G

Y

Y

K

R

M

L

T

I

L

L

I

T

M

M

P

P

D

A

N

S

M

M

S

S

E

M

E

E

R

R

A

V

S

L

I

L

K

K

A

A

Y

F

G

G

A

A

E

E

I

L

I

V

L

L

T

T

P

D

A

P

A

A

G

K

S

G

M

M

E

T

A

G

A

A

I

V

D

Q

L

K

A

A

R

E

S

E

-

I

M

L

E

K

A

N

A

T

G

P

E

D

G

A

K

Y

I

M

L

L

D

Q

Q

Q

F

F

A

D

N

N

P

P

D

A

N

N

P

P

R

K

A

I

H

H

Y

Y

E

E

S

T

T

T

G

G

P

P

E

E

I

I

W

W

R

D

D

D

T

T

Q

K

G

G

Q

K

I

V

T

D

H

I

F

F

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V

S

A

S

G

M
x
I

G
|
G

T
|
T

T
x
G

G
|
G

T
|
T

I

I

M

T

G

G

N

V

S

G

R

R

F

F

L

I

K

K

E

E

Q

K

N

N

P

P

N

K

I

T

Q

Q

I

V

I

I

G

G

V

V

Q

E

P

P

E

T

G

E

N

S

S

D

K

I

I

L

P

S

G

G

I

G

R

K

R

P

W

G

P

P

Q

H

E

K

-

I

-

Q

-
x
G

-

I

-

G

-

A

-

G

Y

F

L

I

P

P

K

K

I

N

Y

L

Q

D

A

Q

E

K

R

I

V

M

D

D

R

E

I

V

I

I

D

A

V

I

D

S

Q

S

A

E

T

E

A

A

E

I

E

E

T

T

T

A

R

K

A

Q

L

L

A

A

A

L

R

K

E

E

G

G

I

L

F

M

A

V

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

A

S

A

V

A

A

A

L

I

K

K

L

V

S

A

A

K

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

I

V

A

V

V

I

V

V

F

C
x
P

D

S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

P

V

L

F

F

active site: K54 (= K43), S277 (= S257)
binding pyridoxal-5'-phosphate: K54 (= K43), N85 (= N73), I188 (≠ M175), G189 (= G176), T190 (= T177), G191 (≠ T178), G192 (= G179), T193 (= T180), G233 (vs. gap), S277 (= S257), P304 (≠ C282)

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)
42% identity, 98% coverage: 6:294/296 of query aligns to 7:305/310 of P9WP55

query
sites
P9WP55

I

I

E

T

S

Q

F

L

V

I

G

G

N

R

T

T

P

P

L

L

V

V

R

R

L

L

Q

R

R

R

L

V

P

T

G

D

N

G

T

A

S

V

N

A

T

D

I

I

L

V

A

A

K

K

L

L

E

E

G

F

N

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

D

D

R

R

P

I

A

G

L

V

S

A

M

M

I

L

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Q

H

A

A

A

E

E

A

Q

R

A

G

G

E

L

I

I

K

K

P

P

G

D

D

T

R

I

L

I

I

L

E

E

A

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

A

L

L

A

A

M

M

A

V

A

C

A

A

I

A

K

R

G

G

Y

Y

K

R

M

C

T

V

L

L

I

T

M

M

P

P

D

E

N

T

M

M

S

S

E

L

E

E

R

R

A

M

S

L

I

L

K

R

A

A

Y

Y

G

G

A

A

E

E

I

L

I

I

L

L

T

T

P

P

A

G

A

A

G

D

S

G

M

M

E

S

A

G

A

A

I

I

D

A

L

K

A

A

R

E

S

E

M

L

E

A

A

K

A

T

G

D

E

Q

G

R

K

Y

I

F

L

V

-

P

D

Q

Q

Q

F

F

A

E

N

N

P

P

D

A

N

N

P

P

R

A

A

I

H

H

Y

R

E

V

S

T

T

T

G

A

P

E

E

E

I

V

W

W

R

R

D

D

T

T

Q

D

G

G

Q

K

I

V

T

D

H

I

F

V

V

V

S

A

S

G

M

V

G
|
G

T
|
T

T
x
G

G
|
G

T
|
T

I

I

M

T

G

G

N

V

S

A

R

Q

F

V

L

I

K

K

E

E

Q

R

N

K

P

P

N

S

I

A

Q

R

I

F

I

V

G

A

V

V

Q

E

P

P

E

A

G

A

N

S

S

P

K

V

I

L

P

S

G

G

I

G

R

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R

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W

G

P

P

Q

H

E

P

-

I

-

Q

-

G

-

I

-

G

-

A

-

G

Y

F

L

V

P

P

K

P

I

V

Y

L

Q

D

A

Q

E

D

R

L

V

V

D

D

R

E

I

I

D

T

V

V

D

G

Q

N

A

E

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D

A

A

E

L

E

N

T

V

T

A

R

R

A

R

L

L

A

A

A

R

R

E

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

T

S

V

V

A

A

A

L

L

K

Q

L

V

S

A

A

R

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

I

V

V

I

V

V

L

C

P

D

D

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

P

V

L

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F

K44 (= K43) modified: N6-(pyridoxal phosphate)lysine
N74 (= N73) binding pyridoxal 5'-phosphate
GTGGT 178:182 (≠ GTTGT 176:180) binding pyridoxal 5'-phosphate
S266 (= S257) binding pyridoxal 5'-phosphate

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)
42% identity, 98% coverage: 6:294/296 of query aligns to 7:305/306 of 2q3dA

query
sites
2q3dA

I

I

E

T

S

Q

F

L

V

I

G

G

N

R

T

T

P

P

L

L

V

V

R

R

L

L

Q

R

R

R

L

V

P

T

G

D

N

G

T

A

S

V

N

A

T

D

I

I

L

V

A

A

K

K

L

L

E

E

G

F

N

F

N

N

P

P

A

A

G

N

S

S

I

V

K
|
K

D

D

R

R

P

I

A

G

L

V

S

A

M

M

I

L

K

Q

H

A

A

A

E

E

A

Q

R

A

G

G

E

L

I

I

K

K

P

P

G

D

D

T

R

I

L

I

I

L

E

E

A

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

I

A

A

L

L

A

A

M

M

A

V

A

C

A

A

I

A

K

R

G

G

Y

Y

K

R

M

C

T

V

L

L

I

T

M

M

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P

D

E

N

T

M

M

S

S

E

L

E

E

R

R

A

M

S

L

I

L

K

R

A

A

Y

Y

G

G

A

A

E

E

I

L

I

I

L

L

T

T

P

P

A

G

A

A

G

D

S

G

M

M

E

S

A

G

A

A

I

I

D

A

L

K

A

A

R

E

S

E

M

L

E

A

A

K

A

T

G

D

E

Q

G

R

K

Y

I

F

L

V

-

P

D

Q

Q
|
Q

F

F

A

E

N

N

P

P

D

A

N

N

P

P

R

A

A

I

H

H

Y

R

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V

S

T

T

T

G

A

P

E

E

E

I

V

W

W

R

R

D

D

T

T

Q

D

G

G

Q

K

I

V

T

D

H

I

F

V

V

V

S

A

S

G

M
x
V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

I

I

M

T

G

G

N

V

S

A

R

Q

F

V

L

I

K

K

E

E

Q

R

N

K

P

P

N

S

I

A

Q

R

I

F

I

V

G

A

V

V

Q

E

P

P

E

A

G

A

N

S

S

P

K

V

I

L

P

S

G

G

I

G

R

Q

R

K

W

G

P

P

Q

H

E

P

-

I

-

Q

-
x
G

-
x
I

-

G

-

A

-

G

Y

F

L

V

P

P

K

P

I

V

Y

L

Q

D

A

Q

E

D

R

L

V

V

D

D

R

E

I

I

D

T

V

V

D

G

Q

N

A

E

T

D

A

A

E

L

E

N

T

V

T

A

R

R

A

R

L

L

A

A

A

R

R

E

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

T

S

V

V

A

A

A

L

L

K

Q

L

V

S

A

A

R

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

I

V

V

I

V

V

L

C
x
P

D
|
D

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

P

V

L

F

F

active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K43), T71 (= T70), S72 (= S71), N74 (= N73), T75 (= T74), Q144 (= Q142), V177 (≠ M175), G178 (= G176), T179 (= T177), G180 (≠ T178), T182 (= T180), G222 (vs. gap), I223 (vs. gap), S266 (= S257), P293 (≠ C282), D294 (= D283)

P47999 Cysteine synthase, chloroplastic/chromoplastic; At.OAS.7-4; Beta-substituted Ala synthase 2;1; ARAth-Bsas2;1; CSase B; AtCS-B; CS-B; O-acetylserine (thiol)-lyase; O-acetylserine sulfhydrylase; OAS-TL B; cpACS1; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 97% coverage: 9:294/296 of query aligns to 82:378/392 of P47999

query
sites
P47999

F

L

V

I

G

G

N

K

T

T

P

P

L

M

V

V

R

Y

L

L

Q

N

R

N

L

V

P

V

G

K

N

G

T

C

S

V

N

A

T

S

I

V

L

A

A

A

K

K

L

L

E

E

G

I

N

M

N

E

P

P

A

C

G

C

S

S

I

V

K

K

D

D

R

R

P

I

A

G

L

Y

S

S

M

M

I

I

K

T

H

D

A

A

E

E

A

E

R

K

G

G

E

L

I

I

K

T

P

P

G

G

D

K

R

S

-

V

L

L

I

V

E

E

A

S

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

G

L

L

A

A

M

F

A

I

A

A

I

S

K

K

G

G

Y

Y

K

K

M

L

T

I

L

L

I

T

M

M

P

P

D

A

N

S

M

M

S

S

E

L

E

E

R

R

A

V

S

L

I

L

K

R

A

A

Y

F

G

G

A

A

E

E

I

L

I

V

L

L

T

T

P

E

A

P

A

A

G

K

S

G

M

M

E

T

A

G

A

A

I

I

D

Q

L

K

A

A

R

E

S

E

-

I

M

L

E

K

A

K

A

T

G

P

E

N

G

S

K

Y

I

M

L

L

D

Q

Q

Q

F

F

A

D

N

N

P

P

D

A

N

N

P

P

R

K

A

I

H

H

Y

Y

E

E

S

T

T

T

G

G

P

P

E

E

I

I

W

W

R

E

D

D

T

T

Q

R

G

G

Q

K

I

I

T

D

H

I

F

L

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V

S

A

S

G

M

I

G

G

T

T

T

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G

G

T

T

I

I

M

T

G

G

N

V

S

G

R

R

F

F

L

I

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K

E

E

Q

R

N

K

P

P

N

E

I

L

Q

K

I

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I

I

G

G

V

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Q

E

P

P

E

T

G

E

N

S

S

A

K

I

I

L

P

S

G

G

I

G

R

K

R

P

W

G

P

P

Q

H

E

K

-

I

-

Q

-

G

-

I

-

G

-

A

-

G

Y

F

L

V

P

P

K

K

I

N

Y

L

Q

D

A

L

E

A

R

I

V

V

D

D

R

E

I

Y

I

I

D

A

V

I

D

S

Q

S

A

E

T

E

A

A

E

I

E

E

T

T

T

S

R

K

A

Q

L

L

A

A

A

L

R

Q

E

E

G

G

I

L

F

L

A

V

G

G

I

I

S

S

G

G

G

A

A

A

V

A

S

A

V

A

A

A

L

I

K

Q

L

V

S

A

A

K

E

R

L

P

E

E

N

N

A

A

-

G

-

K

V

L

I

I

V

A

V

V

I

V

V

F

C

P

D

S

R

F

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

Q

V

L

F

F

Sites not aligning to the query:

61 modified: N-acetylalanine

P0ABK5 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5; EC 2.5.1.47; EC 4.5.1.5 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 96% coverage: 10:294/296 of query aligns to 12:312/323 of P0ABK5

query
sites
P0ABK5

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

Q

N

R

R

L

I

P

-

G

G

N

N

T

-

S

-

N

G

T

R

I

I

L

L

A

A

K

K

L

V

E

E

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S

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R

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N

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P

A

S

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F

S

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|
K

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C

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R

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I

A

G

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A

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M

M

I

I

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W

H

D

A

A

E

E

A

K

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R

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G

E

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I

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P

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G

D

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R

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L

L

I

V

E

E

A

P

T

T

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S

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G

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N

T

T

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G

I

I

A

A

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L

A

A

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A

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A

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Y

K

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M

L

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T

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M

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P

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E

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T

M

M

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S

E

I

E

E

R

R

A

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S

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I

L

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K

A

A

Y

L

G

G

A

A

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N

I

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I

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L

L

T

T

P

E

A

G

A

A

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G

M

M

E

K

A

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A

A

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A

A

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E

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I

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A

A

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N

E

P

G

E

K

K

-

Y

-

L

I

L

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D

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Q

Q

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F

A

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N

N

P

P

D

A

N

N

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E

A

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E

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S

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G

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P

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D

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G

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T

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G

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E

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G

N

K

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D

I

L

I

I

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S

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V

Q

A

P

V

E

E

-

P

-

T

-

D

-

S

-

P

-

V

-

I

-

A

-

Q

-

A

-

L

-

A

-

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-

E

-

I

-

K

-

P

G

G

N

P

S

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K

I

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G

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G

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G

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-

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-

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-

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F

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I

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A

I

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Y

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D

A

L

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K

R

L

V

V

D

D

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K

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N

A

E

T

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A

A

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E

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T

T

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A

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R

A

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L

A

M

A

E

R

E

E

E

G

G

I

I

F

L

A

A

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G

I

I

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S

G

G

G

A

A

A

V

V

S

A

V

A

A

A

L

L

K

K

L

L

S

Q

A

E

E

D

-

E

-

S

L

F

E

T

N

N

A

K

V

N

I

I

V

V

I

I

V

L

C

P

D

S

R

S

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

A

V

L

F

F

K42 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
41% identity, 97% coverage: 8:294/296 of query aligns to 13:310/341 of Q93244

query
sites
Q93244

S

A

F

L

V

I

G

G

N

N

T

T

P

P

L

M

V

V

R

Y

L

I

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L

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N

G

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A

A

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K

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I

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E

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Y

N

M

N

N

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P

A

A

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G

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S

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K

D

D

R

R

P

I

A

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L

A

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A

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M

I

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A

H

A

A

A

E

E

A

K

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D

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G

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I

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P

G

G

-

V

D

T

R

T

L

L

I

I

E

E

A
x
P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

A

L

L

A

A

M

F

A

V

A
|
A

A

A

I

A

K

K

G

G

Y

Y

K

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M

C

T

I

L

V

I

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M

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A

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M

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S

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E

E

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A

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K

A

A

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A

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E

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L

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A

P

A

A

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G

M

M

E

K

A

G

A

A

I

I

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D

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M

A

A

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N

S

Q

M

L

E

K

A

E

A

N

G

I

E

P

G

G

K
x
S

I

I

-

I

L

L

D

A

Q

Q

F

F

A

D

N

N

P

P

D

N

N

N

P

P

R

L

A

V

H

H

Y

Y

E

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S

T

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T

G

G

P

P

E

E

I

I

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W

R

R

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T

T

Q

K

G

G

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T

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H

A

F

V

V

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F

S
x
G

M

V

G
|
G

T

T

T

G

G

G

T

T

I

I

M

T

G

G

N

V

S

G

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K

Q

E

E

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G

A

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V

Q

E

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P

E

E

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E

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S

A

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I

I

L

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S

G

G

I

R

R

P

R

A

W

G

P

P

Q

H

E

K

-

I

-

Q

-

G

-

I

-
x
G

-

A

-

G

Y

F

L

A

P

P

K

A

I

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Y

L

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D

A

T

E

K

R

I

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Y

D

E

R

D

I

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I

I

D

R

V

I

D

H

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S

A

D

T

E

A

A

E

I

E

V

T

M

T

A

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Q

A
x
R

L

L

A

S

A

Y

R

E

E

E

G

G

I

L

F

L

A

G

G

G

I

I

S

S

S
|
S

G

G

G

A

A

N

V

V

S

A

V

A

A

A

L

L

K

Q

L

L

S

A

A

A

E

R

L

P

E

E

N

M

A

A

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G

I

K

V

L

V

I

I

V

V
x
T

C

C

-

L

-

P

D

S

R

C

G

G

D

E

R

R

Y

Y

L

M

S

T

T

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L

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Y

P75 (≠ A69) mutation to L: In n5537; severe loss of protein stability.
A88 (= A82) mutation to V: In n5522; severe loss of protein stability.
S144 (≠ K138) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
G181 (≠ S174) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
G183 (= G176) mutation to R: In n5515; severe loss of protein stability.
G229 (vs. gap) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
R259 (≠ A245) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
S272 (= S258) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
T295 (≠ V281) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.

P0A1E3 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; EC 2.5.1.47 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
44% identity, 99% coverage: 2:294/296 of query aligns to 4:312/323 of P0A1E3

query
sites
P0A1E3

I

I

Y

Y

P

E

T

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I

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E

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T

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I

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G

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A

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N

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T

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S

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G

N
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N

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T

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G

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I

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A

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L

A

A

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Y

A

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A

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A

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G

A

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I

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E

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A

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A

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A

A

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G

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K

-

Y

-

L

I

L

L

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F

A

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N

N

P

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A

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N

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E

A

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E

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P

E

E

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T

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D

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G

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Q

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T

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Y

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K

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D

I

L

I

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T

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V

Q

A

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V

E

E

-

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-

T

-

D

-

S

-

P

-

V

-

I

-

A

-

Q

-

A

-

L

-

A

-

G

-

E

-

I

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K

-

P

G

G

N

P

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H

K

K

I

I

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G

G

I

I

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G

R

A

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G

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-

Q

-

E

-

Y

F

L

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G

I

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Y

L

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D

A

L

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K

R

L

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I

D

D

R

K

I

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D

G

V

I

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N

A

E

T

E

A

A

E

I

E

S

T

T

T

A

R

R

A

R

L

L

A

M

A

E

R

E

E

E

G

G

I

I

F

L

A

A

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

V

S

A

V

A

A

A

L

L

K

K

L

L

S

Q

A

E

E

D

-

E

-

S

L

F

E

T

N

N

A

K

V

N

I

I

V

V

I

I

V

L

C

P

D

S

R

S

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

A

V

L

F

F

N72 (= N73) binding pyridoxal 5'-phosphate
S273 (= S257) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

6z4nAAA structure of oass complexed with upar inhibitor (see paper)
44% identity, 99% coverage: 2:294/296 of query aligns to 5:313/321 of 6z4nAAA

query
sites
6z4nAAA

I

I

Y

Y

P

E

T

D

I

N

E

S

S

L

F

T

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

Q

N

R

R

L

I

P

-

G

G

N

N

T

-

S

-

N

G

T

R

I

I

L

L

A

A

K

K

L

V

E

E

G

S

N

R

N

N

P

P

A

S

G

F

S

S

I

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K
|
K

D

C

R

R

P

I

A

G

L

A

S

N

M

M

I

I

K

W

H

D

A

A

E

E

A

K

R

R

G

G

E

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I

L

K

K

P

P

G

G

D

V

R

E

L

L

I

V

E

E

A

P

T
|
T

S

S

G
|
G

N
|
N

T
|
T

G

G

I

I

A

A

L

L

A

A

M

Y

A

V

A

A

I

A

K

R

G

G

Y

Y

K

K

M

L

T

T

L

L

I

T

M

M

P

P

D

E

N

T

M

M

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S

E

I

E

E

R

R

A

K

S

L

I

L

K

K

A

A

Y

L

G

G

A

A

E

N

I

L

I

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L

L

T

T

P

E

A

G

A

A

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K

S

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M

M

E

K

A

G

A

A

I

I

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Q

L

K

A

A

R

E

S

E

M

I

E

V

A

A

A

S

G

D

E

P

G

Q

K

K

-

Y

-

L

I

L

L

L

D

Q

Q
|
Q

F
|
F

A

S

N

N

P

P

D

A

N

N

P

P

R

E

A

I

H

H

Y

E

E

K

S

T

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T

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G

P

P

E

E

I

I

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W

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E

D

D

T

T

Q

D

G

G

Q

Q

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V

F

F

V

I

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S

S

G

M
x
V

G
|
G

T
|
T

T
x
G

G

G

T
|
T

I

L

M

T

G

G

N

V

S

T

R

R

F

Y

L

I

K

K

E

G

Q

T

N

K

P

G

N

K

I

T

Q

D

I

L

I

I

G

T

V

V

Q

A

P

V

E

E

-

P

-

T

-

D

-

S

-

P

-

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-

I

-

A

-

Q

-

A

-

L

-

A

-

G

-

E

-

I

-

K

-

P

G

G

N

P

S

H

K

K

I

I

P
x
Q

G
|
G

I
|
I

R

G

R
x
A

W

G

P

-

Q

-

E

-

Y

F

L

I

P

P

K

G

I

N

Y

L

Q

D

A

L

E

K

R

L

V

I

D

D

R

K

I

V

D

G

V

I

D

T

Q

N

A

E

T

E

A

A

E

I

E

S

T

T

T

A

R

R

A

R

L

L

A

M

A

E

R

E

E

E

G

G

I

I

F

L

A

A

G

G

I

I

S
|
S

S

S

G

G

G

A

A

A

V

V

S

A

V

A

A

A

L

L

K

K

L

L

S

Q

A

E

E

D

-

E

-

S

L

F

E

T

N

N

A

K

V

N

I

I

V

V

I

I

V

L

C
x
P

D

S

R

S

G

G

D

E

R

R

Y

Y

L

L

S

S

T

T

G

A

V

L

F

F

binding pyridoxal-5'-phosphate: K43 (= K43), N73 (= N73), V177 (≠ M175), G178 (= G176), T179 (= T177), G180 (≠ T178), T182 (= T180), G230 (= G210), S274 (= S257), P301 (≠ C282)
binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K43), T70 (= T70), G72 (= G72), N73 (= N73), T74 (= T74), Q144 (= Q142), F145 (= F143), Q229 (≠ P209), G230 (= G210), I231 (= I211), A233 (≠ R213)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
42% identity, 96% coverage: 6:289/296 of query aligns to 7:300/300 of 3zeiA

query
sites
3zeiA

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active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
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 (= T70), S72 (= S71), I126 (= I125), Q144 (= Q142), F145 (= F143), K215 (≠ R213), G222 (vs. gap), A225 (vs. gap), F227 (≠ Y218)
binding pyridoxal-5'-phosphate: K44 (= K43), N74 (= N73), V177 (≠ M175), G178 (= G176), T179 (= T177), G180 (≠ T178), T182 (= T180), G222 (vs. gap), S266 (= S257), P293 (≠ C282), D294 (= D283)

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)
42% identity, 96% coverage: 6:289/296 of query aligns to 7:300/300 of 2q3cA

query
sites
2q3cA

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active site: K44 (= K43), S266 (= S257), P293 (≠ C282)
binding : T71 (= T70), S72 (= S71), G73 (= G72), T75 (= T74), M122 (= M121), Q144 (= Q142), K215 (≠ R213), G222 (vs. gap), A225 (vs. gap)

P9WP53 O-phosphoserine sulfhydrylase; OPS sulfhydrylase; CysO-thiocarboxylate-dependent cysteine synthase; Cysteine synthase B; CSase B; O-phosphoserine-specific cysteine synthase; [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase; EC 2.5.1.113 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
42% identity, 99% coverage: 3:296/296 of query aligns to 4:308/323 of P9WP53

query
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P9WP53

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N81 (= N73) binding pyridoxal 5'-phosphate
R220 (= R212) mutation to A: 700-fold decrease in the rate of the first half-reaction using OPS. Affects neither the rate of the first half-reaction using OAS nor the rate of the second half-reaction using sulfide or CysO-COSH.
S265 (= S257) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

319:323 mutation Missing: Decreased lifetime of the alpha-aminoacrylate reaction intermediate, increased susceptibility to oxidation by oxidative agents such as hydrogen peroxide, and partial loss of selectivity towards CysO-COSH as sulfur donor.

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
43% identity, 99% coverage: 1:294/296 of query aligns to 2:308/310 of 4lmbA

query
sites
4lmbA

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F

active site: K46 (= K43), S269 (= S257)
binding cysteine: K46 (= K43), T74 (= T70), S75 (= S71), N77 (= N73), T78 (= T74), M101 (= M97), M125 (= M121), M125 (= M121), Q147 (= Q142), F148 (= F143), Q224 (vs. gap), G225 (vs. gap), G225 (vs. gap), I226 (vs. gap), A228 (vs. gap)
binding pyridoxal-5'-phosphate: K46 (= K43), N77 (= N73), V180 (≠ M175), G181 (= G176), T182 (= T177), G183 (≠ T178), T185 (= T180), G225 (vs. gap), S269 (= S257), P296 (≠ C282)

Query Sequence

>WP_019867406.1 NCBI__GCF_000384075.1:WP_019867406.1
MIYPTIESFVGNTPLVRLQRLPGNTSNTILAKLEGNNPAGSIKDRPALSMIKHAEARGEI
KPGDRLIEATSGNTGIALAMAAAIKGYKMTLIMPDNMSEERRASIKAYGAEIILTPAAGS
MEAAIDLARSMEAAGEGKILDQFANPDNPRAHYESTGPEIWRDTQGQITHFVSSMGTTGT
IMGNSRFLKEQNPNIQIIGVQPEGNSKIPGIRRWPQEYLPKIYQAERVDRIIDVDQATAE
ETTRALAAREGIFAGISSGGAVSVALKLSAELENAVIVVIVCDRGDRYLSTGVFPG

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