SitesBLAST

G3XD01 UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase; UDP-D-GlcNAc3NA N-acetyltransferase; UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid 3-N-acetyltransferase; EC 2.3.1.201 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
34% identity, 84% coverage: 27:184/188 of query aligns to 21:161/191 of G3XD01

query
sites
G3XD01

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K136 (≠ R159) mutation to A: Reduction in catalytic activity.; mutation to R: No effect on catalytic activity.

3igjC Crystal structure of maltose o-acetyltransferase complexed with acetyl coenzyme a from bacillus anthracis
33% identity, 73% coverage: 43:180/188 of query aligns to 57:188/188 of 3igjC

query
sites
3igjC

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binding acetyl coenzyme *a: F84 (vs. gap), N86 (= N67), L92 (≠ G73), F105 (≠ I86), A106 (≠ G87), Y112 (≠ V93), A114 (≠ H95), H116 (= H97), W140 (= W132), G142 (= G134), G143 (≠ S135), N148 (≠ V140), P149 (≠ G141), A160 (≠ G152), S161 (≠ A153), V164 (= V156), T166 (= T158), G176 (≠ V168), G177 (= G169), N178 (≠ A170), P179 (= P171), I183 (= I175), K184 (= K176)

4isxA The crystal structure of maltose o-acetyltransferase from clostridium difficile 630 in complex with acetyl-coa
35% identity, 64% coverage: 61:180/188 of query aligns to 78:186/186 of 4isxA

query
sites
4isxA

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binding acetyl coenzyme *a: F82 (≠ K65), N84 (= N67), L103 (≠ I86), A104 (≠ G87), W138 (= W132), G140 (= G134), G141 (≠ S135), G158 (= G152), A159 (= A153), V174 (= V168), G175 (= G169), I181 (= I175), K182 (= K176)

P07464 Galactoside O-acetyltransferase; GAT; Acetyl-CoA:galactoside 6-O-acetyltransferase; Thiogalactoside acetyltransferase; Thiogalactoside transacetylase; EC 2.3.1.18 from Escherichia coli (strain K12) (see 3 papers)
32% identity, 71% coverage: 52:185/188 of query aligns to 64:192/203 of P07464

query
sites
P07464

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S71 (≠ T59) binding
N85 (≠ H71) binding in other chain; binding in other chain
D93 (vs. gap) binding
H115 (= H97) mutation to A: Results in an 1800-fold decrease in catalytic activity.
S142 (= S135) binding in other chain
A160 (= A153) binding in other chain
TK 165:166 (≠ TR 158:159) binding
R180 (≠ K173) binding
R183 (≠ K176) binding in other chain

Sites not aligning to the query:

1 modified: Initiator methionine, Removed; Partial
17 binding

1krvA Galactoside acetyltransferase in complex with coa and pnp-beta-gal (see paper)
32% identity, 71% coverage: 52:185/188 of query aligns to 63:191/201 of 1krvA

query
sites
1krvA

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binding 4-nitrophenyl beta-D-galactopyranoside: S70 (≠ T59), Y82 (= Y69), N84 (≠ H71), V90 (vs. gap), D92 (vs. gap), L102 (= L85), T112 (≠ H95), H114 (= H97), N123 (≠ H106), G124 (≠ P107), M126 (≠ L120)
binding coenzyme a: A104 (≠ G87), S110 (≠ V93), T112 (≠ H95), H114 (= H97), V116 (= V99), W138 (= W132), G140 (= G134), S141 (= S135), N146 (≠ V140), G158 (= G152), A159 (= A153), T164 (= T158), K165 (≠ R159), V172 (≠ L166), A174 (≠ V168), P177 (= P171), R179 (≠ K173), R182 (≠ K176)

Sites not aligning to the query:

binding 4-nitrophenyl beta-D-galactopyranoside: 16, 25

1kruA Galactoside acetyltransferase in complex with iptg and coenzyme a (see paper)
32% identity, 71% coverage: 52:185/188 of query aligns to 63:191/201 of 1kruA

query
sites
1kruA

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binding coenzyme a: A104 (≠ G87), P105 (≠ S88), S110 (≠ V93), T112 (≠ H95), H114 (= H97), W138 (= W132), G140 (= G134), S141 (= S135), N146 (≠ V140), G158 (= G152), A159 (= A153), K165 (≠ R159), A174 (≠ V168), V176 (≠ A170), P177 (= P171), R182 (≠ K176)
binding 1-methylethyl 1-thio-beta-D-galactopyranoside: S70 (≠ T59), Y82 (= Y69), Y82 (= Y69), N84 (≠ H71), V90 (vs. gap), D92 (vs. gap), L102 (= L85), T112 (≠ H95), H114 (= H97), M126 (≠ L120)

Sites not aligning to the query:

binding 1-methylethyl 1-thio-beta-D-galactopyranoside: 16, 17, 22, 25, 25, 26, 62

1krrA Galactoside acetyltransferase in complex with acetyl-coenzyme a (see paper)
32% identity, 71% coverage: 52:185/188 of query aligns to 63:191/200 of 1krrA

query
sites
1krrA

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binding acetyl coenzyme *a: N84 (≠ H71), I103 (= I86), A104 (≠ G87), P105 (≠ S88), S110 (≠ V93), T112 (≠ H95), H114 (= H97), V116 (= V99), W138 (= W132), G140 (= G134), S141 (= S135), N146 (≠ V140), G158 (= G152), A159 (= A153), I162 (≠ V156), T164 (= T158), V172 (≠ L166), A174 (≠ V168), G175 (= G169), V176 (≠ A170), P177 (= P171), R182 (≠ K176)

3nz2C Crystal structure of hexapeptide-repeat containing-acetyltransferase vca0836 complexed with acetyl co enzyme a from vibrio cholerae o1 biovar eltor
31% identity, 64% coverage: 60:180/188 of query aligns to 68:183/183 of 3nz2C

query
sites
3nz2C

F

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C

T

H
x
F

I

I

G
x
N

A

M

M

N

-

V

-

M

-
x
L

-

D

-

G

S

A

R

P

V

I

V

T

V

I

G

G

D

D

D

H

C

V

L
|
L

I
|
I

G
|
G

S

P

R

S

V

T

T

Q

I

F

V
x
Y

D

T

H
x
A

E

S

H
|
H

G

S

V
x
L

Y

-

R

-

K

-

P

-

S

-

D

D

H

Y

P

R

A

R

S

R

L

Q

P

A

W

W

T

-

P

-

D

-

E

E

R

T

L

I

L

C

Q

-

G

-

K

K

P

P

I

I

I

V

I

I

E

E

K

D

N

D

V

V

W
|
W

I

I

G
|
G

S
x
G

G

N

A

V

I

V

I

I

V
x
N

G

Q

G

G

V

V

T

T

I

I

G

G

E

A

G

R

S

S

V

V

I

V

G
x
A

A
|
A

N
|
N

A

S

V

V

T
x
N

R

Q

D

D

I

V

S

P

R

P

Y

D

S

T

L
|
L

A

V

V
x
G

G
|
G

A
x
T

P
|
P

A

A

K

R

V

I

I
x
L

K
x
R

T

S

F

L

D

K

E

D

binding acetyl coenzyme *a: F79 (≠ H71), N81 (≠ G73), L87 (vs. gap), L99 (= L85), I100 (= I86), G101 (= G87), Y107 (≠ V93), A109 (≠ H95), H111 (= H97), L113 (≠ V99), W135 (= W132), G137 (= G134), G138 (≠ S135), N143 (≠ V140), A155 (≠ G152), A156 (= A153), N161 (≠ T158), L169 (= L166), G171 (≠ V168), G172 (= G169), T173 (≠ A170), P174 (= P171), L178 (≠ I175), R179 (≠ K176)
binding magnesium ion: N157 (= N154), T173 (≠ A170)

3ectA Crystal structure of the hexapeptide-repeat containing- acetyltransferase vca0836 from vibrio cholerae
31% identity, 64% coverage: 60:180/188 of query aligns to 61:176/176 of 3ectA

query
sites
3ectA

F

F

G

G

Q

K

N

T

V

I

K

R

I

I

N

G

D

D

Y

H

C

T

H

F

I

I

G

N

A

M

M

N

-

V

-

M

-

L

-

D

-

G

S

A

R

P

V

I

V

T

V

I

G

G

D

D

D

H

C

V

L

L

I

I

G

G

S

P

R

S

V

T

T

Q

I

F

V

Y

D

T

H

A

E

S

H

H

G

S

V

L

Y

-

R

-

K

-

P

-

S

-

D

D

H

Y

P

R

A

R

S

R

L

Q

P

A

W

W

T

-

P

-

D

-

E

E

R

T

L

I

L

C

Q

-

G

-

K

K

P

P

I

I

I

V

I

I

E

E

K

D

N

D

V

V

W

W

I

I

G

G

S

G

G

N

A

V

I

V

I

I

V

N

G

Q

G
|
G

V

V

T

T

I

I

G

G

E

A

G

R

S

S

V

V

I

V

G

A

A

A

N

N

A

S

V

V

T

N

R

Q

D
|
D

I

V

S

P

R

P

Y

D

S

T

L

L

A

V

V

G

G

G

A

T

P

P

A

A

K

R

V

I

I

L

K

R

T

S

F

L

D

K

E

D

binding calcium ion: G138 (= G142), D156 (= D160)

3nz2J Crystal structure of hexapeptide-repeat containing-acetyltransferase vca0836 complexed with acetyl co enzyme a from vibrio cholerae o1 biovar eltor
32% identity, 63% coverage: 60:178/188 of query aligns to 71:184/185 of 3nz2J

query
sites
3nz2J

F

F

G

G

Q

K

N

T

V

I

K

R

I

I

N

G

D

D

Y

H

C

T

H

F

I

I

G
x
N

A

M

M

N

-

V

-

M

-
x
L

-

D

-

G

S

A

R

P

V

I

V

T

V

I

G

G

D

D

D

H

C

V

L

L

I
|
I

G
|
G

S

P

R

S

V

T

T

Q

I

F

V
x
Y

D

T

H
x
A

E

S

H
|
H

G

S

V
x
L

Y

-

R

-

K

-

P

-

S

-

D

D

H

Y

P

R

A

R

S

R

L

Q

P

A

W

W

T

-

P

-

D

-

E

E

R

T

L

I

L

C

Q

-

G

-

K

K

P

P

I

I

I

V

I

I

E

E

K

D

N

D

V

V

W
|
W

I

I

G
|
G

S
x
G

G

N

A

V

I

V

I

I

V
x
N

G

Q

G

G

V

V

T

T

I

I

G

G

E

A

G

R

S

S

V

V

I

V

G
x
A

A
|
A

N

N

A

S

V

V

T
x
N

R

Q

D

D

I

V

S

P

R

P

Y

D

S

T

L
|
L

A

V

V
x
G

G
|
G

A
x
T

P
|
P

A

A

K

R

V

I

I
x
L

K
x
R

T

S

F

L

binding acetyl coenzyme *a: N84 (≠ G73), L90 (vs. gap), I103 (= I86), G104 (= G87), Y110 (≠ V93), A112 (≠ H95), H114 (= H97), L116 (≠ V99), W138 (= W132), G140 (= G134), G141 (≠ S135), N146 (≠ V140), A158 (≠ G152), A159 (= A153), N164 (≠ T158), L172 (= L166), G174 (≠ V168), G175 (= G169), T176 (≠ A170), P177 (= P171), L181 (≠ I175), R182 (≠ K176)

A1ADJ6 Polysialic acid O-acetyltransferase; Capsule O-acetyl transferase; EC 2.3.1.136 from Escherichia coli O1:K1 / APEC (see paper)
34% identity, 59% coverage: 66:176/188 of query aligns to 184:278/307 of A1ADJ6

query
sites
A1ADJ6

I

V

N

T

D

D

Y

K

C

C

H

N

I

-

G

-

A

-

M

-

S

-

R

-

V

V

V

T

V

I

G

G

D

H

D

D

C

C

L

M

I

I

G

A

S

R

R

D

V

V

T

-

I

-

V

-

D

-

H

-

E

-

H

-

G

-

V

I

Y

L

R

R

K

A

P

S

S

D

D

G

H
|
H

P

P

A

-

S

-

L

I

P

F

W

D

T

I

P

H

P

S

D

K

E

K

R

R

L

I

L

N

Q

W

G

A

K

K

P

D

I

I

E

S

K

S

N

Y

V

V

W
|
W

I

V

G

G

S

R

G

N

A

V

I

S

I

I

V

M

G

K

G

G

V

V

T

S

I

V

G

G

E

S

G

G

S

S

V

V

I

I

G

G

A

Y

N

G

A

S

V

I

V

V

T

T

R

K

D

D

I

V

S

P

R

S

Y

M

S

C

L

A

A

A

V

A

G

G

A

N

P

P

A

A

K

K

V

I

I

I

K

K

H210 (= H106) mutation to A: Loss of activity.
W234 (= W132) mutation to A: Loss of activity.

3dhoA Structure of streptogramin acetyltransferase in complex with an inhibitor
37% identity, 56% coverage: 76:180/188 of query aligns to 59:170/203 of 3dhoA

query
sites
3dhoA

S

D

R

K

V

L

V

K

V

I

G

G

D

K

D

F

C

C

L

S

I

I

G

G

S

P

R

G

V

V

T

T

I

I

V

I

D

M

H

N

E

G

H

A

G

N

V

H

Y

R

R
x
M

K

D

P

G

S

S

D

T

H

Y

P

P

A

F

S

N

L

L

-

F

-

G

-

N

P

G

W

W

T

E

-

K

-

H

-

M

P

P

P

K

D

L

E

D

R

Q

L

L

L

P

Q

I

G
x
K

K

G

P

D

I

T

I

I

E

G

K

N

N

D

V

V

W

W

I

I

G

G

S

K

G

D

A

V

I

V

I

I

V

M

G

P

G

G

V

V

T

K

I

I

G

G

E

D

G

G

S

A

V
x
I

I

V

G
x
A

A

A

N

N

A

S

V

V

T
x
V

R

K

D

D

I

I

S

A

R

P

Y

Y

S

M

L
|
L

A
|
A

V
x
G

G

G

A

N

P
|
P

A

A

K

N

V

E

I
|
I

K
|
K

T

Q

-

R

F

F

D

D

E

Q

binding 6-bromo-N'-[(1Z)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-2-methylquinoline-4-carbohydrazide: M84 (≠ R101), K111 (≠ G122), I139 (≠ V150), A141 (≠ G152), V147 (≠ T158), L155 (= L166), A156 (= A167), G157 (≠ V168), P160 (= P171), I164 (= I175), K165 (= K176)

1kk4A Crystal structure of vat(d) in complex with acetyl-coa (see paper)
37% identity, 56% coverage: 76:180/188 of query aligns to 59:170/205 of 1kk4A

query
sites
1kk4A

S

D

R

K

V

L

V

K

V

I

G

G

D

K

D

F

C

C

L

S

I
|
I

G
|
G

S

P

R

G

V

V

T

T

I

I

V

I

D

M

H

N

E

G

H
x
A

G

N

V
x
H

Y

R

R
x
M

K

D

P

G

S

S

D

T

H

Y

P

P

A

F

S

N

L

L

-

F

-

G

-

N

P

G

W

W

T

E

-

K

-

H

-

M

P

P

P

K

D

L

E

D

R

Q

L

L

L

P

Q

I

G
x
K

K

G

P

D

I

T

I

I

E

G

K

N

N

D

V

V

W
|
W

I

I

G
|
G

S
x
K

G

D

A

V

I

V

I

I

V
x
M

G

P

G

G

V

V

T

K

I

I

G

G

E

D

G

G

S

A

V
x
I

I

V

G
x
A

A
|
A

N

N

A

S

V

V

T
x
V

R
x
K

D

D

I

I

S

A

R

P

Y

Y

S

M

L
|
L

A

A

V
x
G

G
|
G

A

N

P
|
P

A

A

K

N

V

E

I
|
I

K

K

T

Q

-

R

F

F

D

D

E

Q

binding acetyl coenzyme *a: I69 (= I86), G70 (= G87), A80 (≠ H97), H82 (≠ V99), M84 (≠ R101), K111 (≠ G122), W121 (= W132), G123 (= G134), K124 (≠ S135), M129 (≠ V140), I139 (≠ V150), A141 (≠ G152), A142 (= A153), V147 (≠ T158), K148 (≠ R159), L155 (= L166), G157 (≠ V168), G158 (= G169), P160 (= P171), I164 (= I175)

Sites not aligning to the query:

binding acetyl coenzyme *a: 37

P50870 Streptogramin A acetyltransferase; Virginiamycin acetyltransferase D; Vat(D); EC 2.3.1.- from Enterococcus faecium (Streptococcus faecium) (see paper)
37% identity, 56% coverage: 76:180/188 of query aligns to 59:170/209 of P50870

query
sites
P50870

S

D

R

K

V

L

V

K

V

I

G

G

D

K

D

F

C

C

L

S

I

I

G

G

S

P

R

G

V

V

T

T

I

I

V

I

D

M

H

N

E

G

H

A

G

N

V
x
H

Y

R

R

M

K

D

P

G

S

S

D

T

H

Y

P

P

A

F

S

N

L

L

-

F

-

G

-

N

P

G

W

W

T

E

-

K

-

H

-

M

P

P

P

K

D

L

E

D

R

Q

L

L

L

P

Q

I

G

K

K

G

P

D

I

T

I

I

E

G

K

N

N

D

V

V

W

W

I

I

G

G

S

K

G

D

A

V

I

V

I

I

V

M

G

P

G

G

V

V

T

K

I

I

G

G

E

D

G

G

S

A

V

I

I

V

G

A

A

A

N

N

A

S

V

V

T

V

R

K

D

D

I

I

S

A

R

P

Y

Y

S

M

L

L

A

A

V

G

G

G

A

N

P

P

A

A

K

N

V

E

I

I

K

K

T

Q

-

R

F

F

D

D

E

Q

H82 (≠ V99) mutation to A: 105-fold decrease in activity.

1mrlA Crystal structure of streptogramin a acetyltransferase with dalfopristin (see paper)
37% identity, 56% coverage: 76:180/188 of query aligns to 59:170/204 of 1mrlA

query
sites
1mrlA

S

D

R

K

V

L

V

K

V

I

G

G

D

K

D

F

C

C

L

S

I

I

G

G

S

P

R

G

V

V

T

T

I

I

V

I

D

M

H

N

E
x
G

H

A

G
x
N

V
x
H

Y

R

R

M

K

D

P

G

S

S

D

T

H

Y

P

P

A

F

S

N

L
|
L

-

F

-

G

-

N

P

G

W

W

T

E

-

K

-

H

-
x
M

P
|
P

P

K

D

L

E

D

R

Q

L
|
L

L

P

Q

I

G

K

K

G

P

D

I

T

I

I

E

G

K

N

N

D

V

V

W

W

I

I

G

G

S

K

G

D

A

V

I

V

I

I

V

M

G

P

G

G

V

V

T

K

I

I

G

G

E

D

G

G

S

A

V

I

I

V

G

A

A

A

N

N

A

S

V

V

T

V

R

K

D

D

I

I

S

A

R

P

Y

Y

S

M

L

L

A

A

V

G

G

G

A

N

P

P

A

A

K

N

V

E

I

I

K

K

T

Q

-

R

F

F

D

D

E

Q

binding 5-(2-diethylamino-ethanesulfonyl)-21-hydroxy-10-isopropyl-11,19-dimethyl-9,26-dioxa-3,15,28-triaza-tricyclo[23.2.1.00,255]octacosa-1(27),12,17,19,25(28)-pentaene-2,8,14,23-tetraone: G79 (≠ E96), N81 (≠ G98), H82 (≠ V99), L93 (= L110), M102 (vs. gap), P103 (= P114), L108 (= L119)

Sites not aligning to the query:

binding 5-(2-diethylamino-ethanesulfonyl)-21-hydroxy-10-isopropyl-11,19-dimethyl-9,26-dioxa-3,15,28-triaza-tricyclo[23.2.1.00,255]octacosa-1(27),12,17,19,25(28)-pentaene-2,8,14,23-tetraone: 14, 17, 37, 39, 54, 56

1khrA Crystal structure of vat(d) in complex with virginiamycin and coenzyme a (see paper)
37% identity, 56% coverage: 76:180/188 of query aligns to 59:170/206 of 1khrA

query
sites
1khrA

S

D

R

K

V

L

V

K

V

I

G

G

D

K

D

F

C

C

L

S

I

I

G

G

S

P

R

G

V

V

T

T

I

I

V

I

D

M

H

N

E
x
G

H
x
A

G
x
N

V
x
H

Y

R

R
x
M

K

D

P

G

S

S

D

T

H

Y

P

P

A

F

S
x
N

L
|
L

-

F

-

G

-

N

P

G

W

W

T

E

-

K

-

H

-
x
M

P
|
P

P

K

D

L

E

D

R

Q

L

L

L

P

Q

I

G

K

K

G

P

D

I

T

I

I

E

G

K

N

N

D

V

V

W
|
W

I

I

G
|
G

S
x
K

G

D

A

V

I

V

I

I

V
x
M

G

P

G

G

V

V

T

K

I

I

G

G

E

D

G

G

S

A

V

I

I

V

G
x
A

A
|
A

N

N

A

S

V

V

T
x
V

R

K

D

D

I

I

S

A

R

P

Y

Y

S

M

L
|
L

A

A

V
x
G

G
|
G

A

N

P
|
P

A

A

K

N

V

E

I
|
I

K

K

T

Q

-

R

F

F

D

D

E

Q

binding coenzyme a: A80 (≠ H97), H82 (≠ V99), M84 (≠ R101), W121 (= W132), G123 (= G134), K124 (≠ S135), M129 (≠ V140), A141 (≠ G152), A142 (= A153), V147 (≠ T158), L155 (= L166), G157 (≠ V168), G158 (= G169), P160 (= P171), I164 (= I175)
binding virginiamycin m1: G79 (≠ E96), A80 (≠ H97), N81 (≠ G98), H82 (≠ V99), N92 (≠ S109), L93 (= L110), M102 (vs. gap), P103 (= P114)

Sites not aligning to the query:

binding virginiamycin m1: 17, 37, 39, 54

6pxaE The crystal structure of chloramphenicol acetyltransferase-like protein from vibrio fischeri es114 in complex with taurocholic acid
32% identity, 63% coverage: 71:188/188 of query aligns to 64:185/221 of 6pxaE

query
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binding taurocholic acid: F65 (≠ I72), Q91 (≠ G98), G92 (≠ V99), F101 (≠ L110), P102 (= P111), F103 (≠ W112), S104 (≠ T113), E107 (≠ D116), F108 (vs. gap), F116 (≠ L119)

Sites not aligning to the query:

binding taurocholic acid: 10, 11, 12, 13, 30, 32

5ux9A The crystal structure of chloramphenicol acetyltransferase from vibrio fischeri es114
32% identity, 63% coverage: 71:188/188 of query aligns to 59:180/215 of 5ux9A

query
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Sites not aligning to the query:

binding magnesium ion: 202, 205

6x3jA Crystal structure of streptogramin a acetyltransferase vata from staphylococcus aureus in complex with streptogramin analog f0224 (46) (see paper)
32% identity, 60% coverage: 76:188/188 of query aligns to 58:178/206 of 6x3jA

query
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binding (2R)-2-[(3S,4R,5E,10E,12E,14S,16R,26aR)-16-fluoro-14-hydroxy-4,12-dimethyl-1,7,22-trioxo-4,7,8,9,14,15,16,17,24,25,26,26a-dodecahydro-1H,3H,22H-21,18-(azeno)pyrrolo[2,1-c][1,8,4,19]dioxadiazacyclotetracosin-3-yl]propyl isoquinolin-3-ylcarbamate: G78 (≠ E96), A79 (≠ H97), H81 (≠ V99), H91 (≠ S109), L92 (= L110), M101 (≠ T113), P102 (= P114), L107 (= L119)
binding thioacetic acid s-{2-[3-(2-hydroxy-3,3-dimethyl-4-phosphonooxy-butyrylamino)-propionylamino]-ethyl} ester: G69 (= G87), P70 (≠ S88), A79 (≠ H97), N80 (≠ G98), H81 (≠ V99), M83 (≠ R101), W120 (= W132), G122 (= G134), A140 (≠ G152), A141 (= A153), I154 (≠ L166)

Sites not aligning to the query:

Query Sequence

>GFF4893 FitnessBrowser__WCS417:GFF4893
MWIRLAFFSVLSKLLYGMNVRVIKGFARVINKGHLQFGSRFTAGVDLRIEVLEDSACVTF
GQNVKINDYCHIGAMSRVVVGDDCLIGSRVTIVDHEHGVYRKPSDHPASLPWTPPDERLL
QGKPIIIEKNVWIGSGAIIVGGVTIGEGSVIGANAVVTRDISRYSLAVGAPAKVIKTFDE
GGKQWLCV

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