SitesBLAST

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
31% identity, 96% coverage: 5:186/189 of query aligns to 8:229/555 of Q8IJR9

query
sites
Q8IJR9

K

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C

Y18 (≠ F15) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (= H17) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
K24 (≠ R21) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
R25 (≠ T22) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C79) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
Q93 (= Q83) binding L-glutamine
C113 (≠ E103) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
K160 (vs. gap) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
W167 (= W125) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S127) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D130) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H166) binding L-glutamine
Y212 (≠ S170) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H171) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.

Sites not aligning to the query:

336 binding XMP
371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
476 binding XMP
539 R→L: 85 percent decrease in glutaminase activity.
547 binding XMP; K→L: 85 percent decrease in glutaminase activity.
552 binding XMP
553 binding XMP; E→L: 85 percent decrease in glutaminase activity.
555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
30% identity, 96% coverage: 5:186/189 of query aligns to 2:218/525 of 4wioA

query
sites
4wioA

K

K

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active site: G52 (= G55), A83 (≠ C79), Y84 (≠ L80), H197 (= H166), E199 (= E168)
binding glutamine: Q87 (= Q83), N158 (≠ S127), H159 (= H128), N160 (≠ A129), D161 (= D130), H197 (= H166)

Sites not aligning to the query:

active site: 255, 393

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
29% identity, 98% coverage: 2:186/189 of query aligns to 2:191/673 of 8hx8A

query
sites
8hx8A

R

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binding magnesium ion: I175 (≠ S170), S177 (≠ T172)

Sites not aligning to the query:

binding magnesium ion: 521, 655, 658
binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614

2vxoB Human gmp synthetase in complex with xmp (see paper)
33% identity, 94% coverage: 6:183/189 of query aligns to 6:182/658 of 2vxoB

query
sites
2vxoB

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active site: G55 (= G55), C82 (= C79), Y83 (≠ L80), H165 (= H166), E167 (= E168)

Sites not aligning to the query:

active site: 223, 381
binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
33% identity, 96% coverage: 5:186/189 of query aligns to 1:183/477 of 3uowB

query
sites
3uowB

K

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C

active site: G47 (= G55), C67 (= C79), Y68 (≠ L80), H162 (= H166), E164 (= E168)

Sites not aligning to the query:

active site: 218, 340
binding xanthosine-5'-monophosphate: 288, 363, 364, 365, 405, 469, 473, 474, 475

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
32% identity, 94% coverage: 6:183/189 of query aligns to 28:207/693 of P49915

query
sites
P49915

I

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P

P

N

L

V

E

T

T

P

P

I

A

E

F

E

A

I

I

L

K

A

E

E

Q

E

G

P

F

D

R

G

A

L

I

I

I

L

I

S

S

G

G

P

P

E

N

M

S

E

V

R

Y

A

A

-

E

-

D

G

A

L

P

C

W

F

F

D

D

-

P

Y

A

V

I

R

F

E

T

I

I

D

G

V

K

P

P

I

V

L

L

G

G

I

I

C
|
C

L

Y

G

G

H

M

Q

Q

A

M

I

M

A

N

L

K

A

V

Y

F

G

G

H

T

V

V

H

H

A

K

G

K

K

S

K

V

G

R

G

E

Y

D

A

G

E

V

I

F

E

N

V

I

E

S

V

V

L

D

E

N

E

T

D

C

D

S

I

L

L

F

R

R

G

G

L

L

G

Q

P

K

K

E

T

E

T

V

V

V

W

L

A

L

S

T

H

H

A

G

D

D

E

S

V

V

A

D

I

K

L

V

P

A

D

D

G

G

F

F

I

K

H

V

L

V

A

A

R

R

S

S

D

G

V

N

C

I

E

-

I

V

E

A

A

G

M

I

R

A

H

N

P

E

T

S

K

K

P

K

I

L

Y

Y

G

G

V

A

Q

Q

W

F

H
|
H

P

P

E
|
E

V

V

S

G

H

L

T

T

K

E

K

N

G

G

E

K

E

V

L

I

L

L

M

K

N

N

F

F

F

L

C104 (= C79) active site, For GATase activity
H190 (= H166) active site, For GATase activity
E192 (= E168) active site, For GATase activity

Sites not aligning to the query:

337 binding XMP
522 binding XMP
610 binding XMP
685 binding XMP
691 binding XMP

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
33% identity, 94% coverage: 6:183/189 of query aligns to 2:185/187 of P00903

query
sites
P00903

I

I

L

L

V

L

V

I

N

D

N

N

Y

Y

G

D

Q

S

F

F

C

T

H

W

L

N

I

L

H

Y

R

Q

T

Y

V

F

R

C

D

E

L

L

D

G

M

A

D

D

T

V

K

L

I

V

I

K

P

R

N

N

-

D

V

A

T

L

P

T

I

L

E

A

E

D

I

I

L

D

A

A

E

L

E

K

P

P

D

Q

G

K

L

I

I

V

L

I

S

S

G

P

G

G

P

P

-

C

E

T

M

P

E

D

R

E

A

A

G

G

L

I

C

S

F

L

D

D

Y

V

V

I

R

R

E

H

I

Y

-

A

-

G

D

R

V

L

P

P

I

I

L

L

G

G

I

V

C
|
C

L

L

G

G

H

H

Q

Q

A

A

I

M

A

A

L

Q

A

A

Y

F

G

G

H

K

V

V

H

V

A

R

G

A

K

A

K

K

G

V

G

M

Y

H

A

G

E

K

I

T

E

S

V

P

E

I

V

T

L

H

E

N

E

G

D

E

D

G

I

V

L

F

R

R

G

G

L

L

G

A

P

N

K

P

T

L

T

T

V

V

W

T

A

R

S

Y

H

H

A

S

-

L

-

V

D

V

E

E

V

P

A

D

I

S

L

L

P

P

D

A

G

C

F

F

I

D

H

V

L

T

A

A

R

W

S

S

D

E

V

T

C

R

E

E

I

I

E

M

A

G

M

I

R

R

H

H

P

R

T

Q

K

W

P

D

I

L

Y

E

G

G

V

V

Q

Q

W

F

H
|
H

P

P

E
|
E

V

S

S

I

H

L

T

S

K

E

K

Q

G

G

E

H

E

Q

L

L

M

A

N

N

F

F

F

L

C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H166) mutation to Q: Loss of activity.
E170 (= E168) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 96% coverage: 6:187/189 of query aligns to 75:268/276 of Q42565

query
sites
Q42565

I

I

L

I

V

V

V

I

N

D

N

N

Y

Y

G

D

Q

S

F

F

C

T

H

Y

L

N

I

L

H

C

R

Q

T

Y

V

M

R

G

D

E

L

L

D

G

M

C

D

H

T

F

K

E

I

V

I

Y

P

R

N

N

-

D

V

E

T

L

P

T

I

V

E

E

I

L

L

K

A

K

E

K

E

N

P

P

D

R

G

G

L

V

I

L

L

I

S

S

G

P

G

G

P

P

E

G

M

T

-

P

E

Q

R

D

A

S

G

G

L

I

C

S

F

L

D

Q

Y

T

V

V

R

L

E

E

I

L

D

G

-

P

-

L

V

V

P

P

I

L

L

F

G
|
G

I

V

C

C

L

M

G

G

H

L

Q

Q

A

C

I

I

A

G

L

E

A

A

Y

F

G

G

H

K

V

I

H

V

A

R

G

S

K

P

-

F

-

G

-

V

-

M

K

H

G
|
G

G

K

Y

S

A

S

E

M

I

V

E

H

V

Y

E

D

V

E

L

K

E

G

E

E

D

E

D

G

I

L

L

F

R

S

G

G

L

L

G

S

P

N

K

P

T

F

T

I

V

V

W

G

A

R

S

Y

H

H

A

S

D

-

E

-

V

L

A

V

I

I

L

E

P

K

D

D

G

T

F

F

I

P

H

S

-

D

-

E

-

L

-

E

-

V

L

T

A

A

R

W

S

T

D

E

V

D

C

G

E

L

I

V

E

M

A

A

M

A

R

R

H

H

P

R

T

K

-

Y

K

K

P

H

I

I

Y

Q

G

G

V

V

Q

Q

W

F

H

H

P

P

E

E

V

S

S

I

H

I

T

T

K

T

K

E

G

G

E

K

E

T

L

I

L

V

M

R

N

N

F

F

F

I

E

K

V

I

C

V

D

E

G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G99) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
29% identity, 90% coverage: 19:189/189 of query aligns to 204:376/379 of 1ce8B

query
sites
1ce8B

I

I

H

L

R

R

T

M

V

L

R

V

D

D

L

R

D

G

M

C

D

R

T

L

K

T

I

I

I

V

P

P

N

A

V

Q

T

T

P

S

I

A

E

E

E

D

I

V

L

L

A

K

E

M

E

N

P

P

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G

G

P

P

-

G

-

D

-

P

-

A

E

P

M

C

E

D

R

Y

A

A

G

I

L

T

C

A

F

I

D

Q

Y

K

V

F

R

L

E

E

I

T

D

D

V

I

P

P

I

V

L

F

G

G

I

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

-

K

-

T

-

V

H

K

V

M

H

K

A

F

G

G

K

H

G

G

Y

N

A

H

E

P

I

V

E

K

V

-

E

-

V

-

L

-

E

-

D

-

D

D

I

V

L

E

R

K

G

N

L

V

G

V

P

M

K

I

T

T

T

A

V

Q

W

N

A

H

S

G

H

F

A

A

D

V

E

D

V

E

A

A

I

T

L

L

P

P

D

A

G

N

F

L

-

R

-

V

I

T

H

H

L

K

A

S

R

L

S

F

D

D

V

-

C

G

E

T

I

L

E

Q

A

G

M

I

R

H

H

R

P

T

T

D

K

K

P

P

I

A

Y

F

G

S

V

F

Q

Q

W

G

H
|
H

P

P

E
|
E

V

A

S

S

-

P

H

G

T

P

K

H

K

D

G

A

E

A

E

P

L

L

L

F

M

D

N

H

F

F

F

I

E

E

V

L

C

I

D

E

L

Q

Y

Y

active site: C268 (= C79), H352 (= H166), E354 (= E168)

Sites not aligning to the query:

binding L-ornithine: 119, 122

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
29% identity, 90% coverage: 19:189/189 of query aligns to 205:377/382 of P0A6F1

query
sites
P0A6F1

I

I

H

L

R

R

T

M

V

L

R

V

D

D

L

R

D

G

M

C

D

R

T

L

K

T

I

I

I

V

P

P

N

A

V

Q

T

T

P

S

I

A

E

E

E

D

I

V

L

L

A

K

E

M

E

N

P

P

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G
|
G

P

P

-
x
G

-

D

-

P

-

A

E

P

M

C

E

D

R

Y

A

A

G

I

L

T

C

A

F

I

D

Q

Y

K

V

F

R

L

E

E

I

T

D

D

V

I

P

P

I

V

L

F

G

G

I

I

C

C

L
|
L

G

G

H

H

Q
|
Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

-

K

-

T

-

V

H

K

V

M

H

K

A

F

G

G

K

H

G

G

Y

N

A

H

E

P

I

V

E

K

V

-

E

-

V

-

L

-

E

-

D

-

D

D

I

V

L

E

R

K

G

N

L

V

G

V

P

M

K

I

T

T

T

A

V

Q

W
x
N

A

H

S
x
G

H
x
F

A

A

D

V

E

D

V

E

A

A

I

T

L

L

P

P

D

A

G

N

F

L

-

R

-

V

I

T

H

H

L

K

A

S

R

L

S

F

D

D

V

-

C

G

E

T

I

L

E

Q

A

G

M

I

R

H

H

R

P

T

T

D

K

K

P

P

I

A

Y

F

G

S

V

F

Q

Q

W

G

H

H

P

P

E

E

V

A

S

S

-

P

H

G

T

P

K

H

K

D

G

A

E

A

E

P

L

L

L

F

M

D

N

H

F

F

F

I

E

E

V

L

C

I

D

E

L

Q

Y

Y

G241 (= G55) binding L-glutamine
G243 (vs. gap) binding L-glutamine
L270 (= L80) binding L-glutamine
Q273 (= Q83) binding L-glutamine
N311 (≠ W125) binding L-glutamine
G313 (≠ S127) binding L-glutamine
F314 (≠ H128) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
25% identity, 98% coverage: 2:186/189 of query aligns to 1:148/632 of 8hx9A

query
sites
8hx9A

R

R

E

H

L

M

K

R

I

T

L

L

V

L

V

I

N

D

N

N

Y

Y

G

D

Q

S

F

F

C

T

H

H

L

N

I

L

H

F

R

Q

T

Y

V

I

R

G

D

E

L

A

D

T

M

G

D

Q

T

P

K

P

I

V

-

V

P

P

N

N

V

D

T

A

P

D

I

W

E

S

E

R

I

L

L

P

A

V

E

E

E

D

P

F

D

D

G

A

L

I

I

V

L

V

S

S

G

-

P

-

E

-

M

-

E

P

R

R

A

A

G

-

L

-

C

-

F

-

D

-

Y

-

V

I

R

T

E

D

I

S

D

G

V

L

P

P

I

V

L

L

G

G

I

V

C

C

L

L

G

M

H

H

Q

-

A

-

I

-

A

-

L

-

A

-

Y

-

G

-

G

G

H

R

V

V

H

S

A

E

G

V

K

R

K

H

G

T

G

G

Y

-

A

-

E

-

I

-

E

-

V

-

E

-

V

-

L

-

E

-

D

E

D

D

I

V

L

F

R

R

G

G

L

L

G

P

P

S

K

P

T

F

T

T

V

A

W

V

A

R

S

Y

H

H

A

-

D

-

E

-

V

-

A

-

I

-

L

-

P

-

D

D

G

E

F

L

I

E

H

P

L

L

A

A

R

W

S

S

D

D

V

D

C

G

E

V

I

V

E

M

A

G

M

L

R

R

H

H

P

R

T

E

K

K

P

P

I

L

Y

W

G

G

V

V

Q

Q

W

F

H

H

P

P

E

E

V

S

S

I

H

G

T
x
S

K
x
D

K

F

G

G

E

R

E

E

L

I

L

M

M

A

N

N

F

F

F

R

E

D

V

L

C

A

binding magnesium ion: S134 (≠ T172), D135 (≠ K173)

Sites not aligning to the query:

binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575

P07258 Carbamoyl phosphate synthase arginine-specific small chain; CPS; CPSase; CPSase-arg; Arginine-specific carbamoyl phosphate synthetase, glutamine chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 78% coverage: 43:189/189 of query aligns to 220:373/411 of P07258

query
sites
P07258

L

V

A

A

E

S

E

E

P

F

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G

G

P

P

-

G

E

N

M

P

E

E

R

L

A

C

G

Q

L

A

C

T

F

I

D

S

Y

N

V

V

R

R

E

E

I

L

-

L

-

N

-

P

-

V

-

Y

-

D

D

C

V

I

P

P

I

I

L

F

G

G

I

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

H

S

V

T

H

H

A

K

G

L

K

K

K

Y

G

G

G

N

Y

R

A

A

E

-

I

-

E

-

V

-

E

H

V

N

L

I

E

P

E

A

D

M

D

D

I

L

L

T

R

T

G

G

L

Q

G

C

P

H

K

I

T

T

T

S

V

Q

W

N

A
x
H

S

G

H

Y

A

A

D

V

E

D

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D

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C264 (= C79) mutation to D: Abolishes glutamine-dependent CPSase activity.
H307 (≠ A126) mutation to D: Abolishes glutamine-dependent CPSase activity.
H349 (= H166) mutation to D: Abolishes glutamine-dependent CPSase activity.

P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
30% identity, 76% coverage: 41:183/189 of query aligns to 208:353/2225 of P08955

query
sites
P08955

E

E

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D

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D

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D

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F

F

Sites not aligning to the query:

1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
28% identity, 90% coverage: 19:189/189 of query aligns to 204:376/379 of 1c3oB

query
sites
1c3oB

I

I

H

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D

D

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D

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D

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D

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x
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G

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x
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x
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L

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S

G

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x
N

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x
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x
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x
F

A

A

D

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D

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A

A

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H

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Y

active site: S268 (≠ C79), H352 (= H166), E354 (= E168)
binding glutamine: N239 (≠ G54), G240 (= G55), G242 (vs. gap), S268 (≠ C79), L269 (= L80), N310 (≠ W125), H311 (≠ A126), G312 (≠ S127), F313 (≠ H128)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
29% identity, 92% coverage: 6:179/189 of query aligns to 4:183/193 of P00900

query
sites
P00900

I

I

L

L

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L

N

D

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A

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D

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G

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L

C84 (= C79) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

Query Sequence

>WP_011033217.1 NCBI__GCF_000007065.1:WP_011033217.1
MRELKILVVNNYGQFCHLIHRTVRDLDMDTKIIPNVTPIEEILAEEPDGLILSGGPEMER
AGLCFDYVREIDVPILGICLGHQAIALAYGGHVHAGKKGGYAEIEVEVLEEDDILRGLGP
KTTVWASHADEVAILPDGFIHLARSDVCEIEAMRHPTKPIYGVQWHPEVSHTKKGEELLM
NFFEVCDLY

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