SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BWI76_RS11780 FitnessBrowser__Koxy:BWI76_RS11780 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)

P77247 Hexitol phosphatase B; 2-deoxyglucose-6-phosphate phosphatase; Mannitol-1-phosphatase; Sorbitol-6-phosphatase; Sugar-phosphatase; EC 3.1.3.68; EC 3.1.3.22; EC 3.1.3.50; EC 3.1.3.23 from Escherichia coli (strain K12) (see paper)
79% identity, 100% coverage: 1:222/222 of query aligns to 1:222/222 of P77247

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D13 (= D13) binding ; mutation to A: Loss of phosphatase activity.
D15 (= D15) binding
D173 (= D173) binding

1te2A Putative phosphatase ynic from escherichia coli k12
79% identity, 98% coverage: 5:222/222 of query aligns to 1:218/218 of 1te2A

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active site: D9 (= D13), D11 (= D15), S17 (= S21), D44 (= D48), S111 (= S115), A112 (= A116), K144 (= K148), E168 (= E172), D169 (= D173)
binding calcium ion: D9 (= D13), D11 (= D15), D169 (= D173)
binding 2-phosphoglycolic acid: D9 (= D13), M10 (= M14), D11 (= D15), G47 (= G51), S111 (= S115), A112 (= A116), K144 (= K148)

Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 84% coverage: 6:191/222 of query aligns to 73:260/1055 of Q8VZ10

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D80 (= D13) mutation to N: Complete rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.

Sites not aligning to the query:

431:434 CINC→SINS: No rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
859 E→K: In soq1-2; high light intensity-dependent and irreversible nonphotochemical quenching (NPQ) due to a decrease in chlorophyll excited-state lifetime.

4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
30% identity, 84% coverage: 6:191/222 of query aligns to 3:191/227 of 4g9bA

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active site: D10 (= D13), L11 (≠ M14), D12 (= D15), T18 (≠ S21), K46 (≠ L50), S117 (= S115), V118 (≠ A116), K148 (= K148), E172 (= E172), D173 (= D173)
binding magnesium ion: D10 (= D13), D12 (= D15), D173 (= D173)

P95649 Protein CbbY; RuCbby; EC 3.1.3.- from Cereibacter sphaeroides (Rhodobacter sphaeroides) (see paper)
31% identity, 97% coverage: 7:222/222 of query aligns to 2:222/230 of P95649

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D10 (= D15) mutation to N: Loss of catalytic activity.
E17 (= E22) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
H20 (≠ W25) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Y42 (≠ M46) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
R54 (≠ V58) mutation to A: 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
K78 (≠ I79) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.

4uasA Crystal structure of cbby from rhodobacter sphaeroides in complex with phosphate (see paper)
31% identity, 97% coverage: 7:222/222 of query aligns to 2:222/225 of 4uasA

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I

L

G

A

L

V

A

A

S
x
T

A
x
T

S

T

P

S

L

L

R

P

M

N

L

V

E

E

-

A

-

L

-

C

K

R

V

A

L

C

T

F

M

G

F

H

E

P

L

A

R

R

D

E

Q

I

F

F

D

D

A

V

L

I

A

A

S

A

A

G

E

D

M

M

L

V

P

A

F

E

S

K

K
|
K

P

P

H

S

P

P

Q

D

V

I

Y

Y

L

R

N

L

C

A

A

L

A

R

S

E

L

L

G

D

V

V

S

P

P

P

M

E

N

R

C

A

V

V

A

A

L

L

E
|
E

D
|
D

S

S

V

L

N

N

G

G

M

L

I

R

A

A

S

A

K

K

A

G

A

A

R

G

M

L

R

R

S

C

I

I

V

V

V

S

P

P

E

-

A

G

E

F

N

Y

S

T

R

R

D

H

P

E

R

E

F

F

V

A

L

G

A

A

D

D

V

R

K

L

L

L

A

D

T

S

L

F

E

A

S

E

L

L

T

-

P

-

G

G

D

G

L

L

L

A

G

G

active site: D8 (= D13), V9 (≠ M14), D10 (= D15), T16 (≠ S21), T47 (≠ G51), T115 (≠ S115), T116 (≠ A116), K151 (= K148), E175 (= E172), D176 (= D173)
binding magnesium ion: D8 (= D13), D10 (= D15), D176 (= D173)
binding phosphate ion: D8 (= D13), V9 (≠ M14), D10 (= D15), T115 (≠ S115), T116 (≠ A116), K151 (= K148)

4uauA Crystal structure of cbby (mutant d10n) from rhodobacter sphaeroides in complex with xylulose-(1,5)bisphosphate, crystal form ii (see paper)
31% identity, 97% coverage: 7:222/222 of query aligns to 2:222/226 of 4uauA

query
sites
4uauA

I

I

H

E

A

A

A

I

I

L

F

F

D
|
D

M
x
V

D
x
N

G

G

L

T

L

L

I

A

D

E

S
x
T

E
|
E

P

E

L

L

W
x
H

D

R

K

R

A

A

E

F

L

N

E

E

V

T

M

F

A

A

S

A

L

L

G

G

V

V

D

D

-

W

I

F

S

W

R

D

R

R

H

E

E

E

M

Y

P

R

D

E

I

L

L

L

G
x
T

L

T

R
x
T

I
x
G

D
x
G

L

K

V

E

V
x
R

D

I

L

A

W

R

F

F

A

L

Q

R

Q

H

P

Q

W

K

K

G

G

D

P

P

D

A

R

P

-

L

-

P

-

I

A

A

E

D

V

I

T
x
H

A

R

R

A

I
x
K

I

T

N

E

R

R

A

F

I

V

Q

A

L

L

V

M

E

A

E

E

A

G

R

E

-

I

P

A

L

L

L

R

P

P

G

G

A

I

R

A

Q

D

A

L

V

I

A

A

L

E

C

A

K

K

A

R

Q

A

G

G

L

I

K

R

I

L

G

A

L

V

A

A

S
x
T

A
x
T

S
x
T

P
x
S

L

L

R

P

M

N

L

V

E

E

-

A

-

L

-

C

K

R

V

A

L

C

T

F

M

G

F

H

E

P

L

A

R

R

D

E

Q

I

F

F

D

D

A

V

L

I

A

A

S

A

A

G

E

D

M

M

L

V

P

A

F

E

S

K

K
|
K

P

P

H

S

P

P

Q

D

V

I

Y

Y

L

R

N

L

C

A

A

L

A

R

S

E

L

L

G

D

V

V

S

P

P

P

M

E

N

R

C

A

V

V

A

A

L

L

E
|
E

D
|
D

S

S

V

L

N

N

G

G

M

L

I

R

A

A

S

A

K

K

A

G

A

A

R

G

M

L

R

R

S

C

I

I

V

V

V

S

P

P

E

-

A

G

E

F

N

Y

S

T

R

R

D

H

P

E

R

E

F

F

V

A

L

G

A

A

D

D

V

R

K

L

L

L

A

D

T

S

L

F

E

A

S

E

L

L

T

-

P

-

G

G

D

G

L

L

L

A

G

G

active site: D8 (= D13), V9 (≠ M14), N10 (≠ D15), T16 (≠ S21), T47 (≠ G51), T115 (≠ S115), T116 (≠ A116), K151 (= K148), E175 (= E172), D176 (= D173)
binding magnesium ion: D8 (= D13), N10 (≠ D15), D176 (= D173)
binding xylulose-1,5-bisphosphate: D8 (= D13), V9 (≠ M14), N10 (≠ D15), E17 (= E22), H20 (≠ W25), T49 (≠ R53), G50 (≠ I54), G51 (≠ D55), R54 (≠ V58), H75 (≠ T76), K78 (≠ I79), T115 (≠ S115), T116 (≠ A116), T117 (≠ S117), S118 (≠ P118)

7ocrB NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
25% identity, 88% coverage: 5:199/222 of query aligns to 7:195/675 of 7ocrB

query
sites
7ocrB

R

K

Q

P

I

V

H

H

A

G

A

A

I

I

F

F

D
|
D

M

M

D
|
D

G

G

L

T

L

M

I

F

D

D

S

T

E

E

P

R

L

L

-

R

W

F

D

Q

K

T

A

L

E

Q

L

Q

E

A

V

S

M

Q

A

E

S

L

L

I

G

G

V

Q

D

E

I

F

S

S

R

H

R

E

H

Y

E

L

M

M

P

-

D

Q

I

C

L

L

G

G

L

L

R

S

I

A

D

T

L

T

V

A

V

E

D

K

L

L

W

-

F

-

A

A

Q

Q

Q

R

P

L

W

Y

K

K

G

-

P

-

D

-

R

-

A

-

E

E

V

I

T

R

A

K

R

R

I

A

I

D

N

E

R

M

A

E

I

L

Q

E

L

H

V

I

E

R

E

K

-

H

A

G

R

V

P

P

L

I

L

K

P

K

G

G

A

L

R

V

Q

Q

A

V

V

L

A

E

L

R

C

L

K

R

A

K

Q

S

G

G

L

L

K

R

I

M

G

A

L

V

A

A

S

T

A

S

S

S

P

R

L

R

R

A

M

I

L

A

E

E

K

E

V

Y

L

L

T

I

M

N

F

A

E

N

L

V

R

Y

D

K

Q

F

F

F

D

D

A

V

L

I

A

T

S

C

A

G

E

D

M

E

L

V

P

E

F

Q

S

G

K

K

P

P

H

H

P

P

Q

E

V

I

Y

F

L

L

N

K

C

A

A

A

A

S

S

Q

L

L

G

H

V

L

S

D

P

A

M

N

N

Q

C

C

V

L

A

M

L

F

E

E

D
|
D

S

S

V

E

N

N

G

G

M

L

I

T

A

S

S

A

K

H

A

T

A

S

R

K

M

G

R

L

S

T

I

I

V

L

P

K

E

D

A

I

E

K

N

E

S

P

R

N

D

D

binding magnesium ion: D15 (= D13), D17 (= D15), D169 (= D173)

Sites not aligning to the query:

binding fructose -6-phosphate: 362, 403, 508, 513, 516, 587, 590, 594, 595, 601
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 244, 246, 247, 248, 273, 274, 329, 330, 333, 361, 362, 406, 587, 590

7ocqA Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
24% identity, 88% coverage: 5:199/222 of query aligns to 7:201/686 of 7ocqA

query
sites
7ocqA

R

K

Q

P

I

V

H

H

A

G

A

A

I

I

F

F

D
|
D

M

M

D
|
D

G

G

L

T

L

M

I

F

D

D

S

T

E

E

P

R

L

L

-

R

W

F

D

Q

K

T

A

L

E

Q

L

Q

E

A

V

S

M

Q

A

E

S

L

L

I

G

G

V

Q

D

E

I

F

S

S

R

H

R

E

H

Y

E

L

M

M

P

-

D

Q

I

C

L

L

G

G

L

L

R

S

I

A

-

T

-

A

-

E

D

K

L

L

V

A

V

Q

D

R

L

L

W

Y

F

G

A

V

Q

D

Q

V

P

P

W

Y

K

K

G

-

P

-

D

-

R

-

A

-

E

E

V

I

T

R

A

K

R

R

I

A

I

D

N

E

R

M

A

E

I

L

Q

E

L

H

V

I

E

R

E

K

-

H

A

G

R

V

P

P

L

I

L

K

P

K

G

G

A

L

R

V

Q

Q

A

V

V

L

A

E

L

R

C

L

K

R

A

K

Q

S

G

G

L

L

K

R

I

M

G

A

L

V

A

A

S

T

A

S

S

S

P

R

L

R

R

A

M

I

L

A

E

E

K

E

V

Y

L

L

T

I

M

N

F

A

E

N

L

V

R

Y

D

K

Q

F

F

F

D

D

A

V

L

I

A

T

S

C

A

G

E

D

M

E

L

V

P

E

F

Q

S

G

K

K

P

P

H

H

P

P

Q

E

V

I

Y

F

L

L

N

K

C

A

A

A

A

S

S

Q

L

L

G

H

V

L

S

D

P

A

M

N

N

Q

C

C

V

L

A

M

L

F

E

E

D
|
D

S

S

V

E

N

N

G

G

M

L

I

T

A

S

S

A

K

H

A

T

A

S

R

K

M

G

R

L

S

T

I

I

V

L

P

K

E

D

A

I

E

K

N

E

S

P

R

N

D

D

binding magnesium ion: D15 (= D13), D17 (= D15), D175 (= D173)

Sites not aligning to the query:

binding [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-4~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-3,4,5-tris(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate: 252, 253, 254, 279, 280, 335, 369, 370

7ocpA NADPH bound to the dehydrogenase domain of the bifunctional mannitol- 1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
24% identity, 88% coverage: 5:199/222 of query aligns to 7:201/688 of 7ocpA

query
sites
7ocpA

R

K

Q

P

I

V

H

H

A

G

A

A

I

I

F

F

D
|
D

M

M

D
|
D

G

G

L

T

L

M

I

F

D

D

S

T

E

E

P

R

L

L

-

R

W

F

D

Q

K

T

A

L

E

Q

L

Q

E

A

V

S

M

Q

A

E

S

L

L

I

G

G

V

Q

D

E

I

F

S

S

R

H

R

E

H

Y

E

L

M

M

P

-

D

Q

I

C

L

L

G

G

L

L

R

S

I

A

-

T

-

A

-

E

D

K

L

L

V

A

V

Q

D

R

L

L

W

Y

F

G

A

V

Q

D

Q

V

P

P

W

Y

K

K

G

-

P

-

D

-

R

-

A

-

E

E

V

I

T

R

A

K

R

R

I

A

I

D

N

E

R

M

A

E

I

L

Q

E

L

H

V

I

E

R

E

K

-

H

A

G

R

V

P

P

L

I

L

K

P

K

G

G

A

L

R

V

Q

Q

A

V

V

L

A

E

L

R

C

L

K

R

A

K

Q

S

G

G

L

L

K

R

I

M

G

A

L

V

A

A

S

T

A

S

S

S

P

R

L

R

R

A

M

I

L

A

E

E

K

E

V

Y

L

L

T

I

M

N

F

A

E

N

L

V

R

Y

D

K

Q

F

F

F

D

D

A

V

L

I

A

T

S

C

A

G

E

D

M

E

L

V

P

E

F

Q

S

G

K

K

P

P

H

H

P

P

Q

E

V

I

Y

F

L

L

N

K

C

A

A

A

A

S

S

Q

L

L

G

H

V

L

S

D

P

A

M

N

N

Q

C

C

V

L

A

M

L

F

E

E

D
|
D

S

S

V

E

N

N

G

G

M

L

I

T

A

S

S

A

K

H

A

T

A

S

R

K

M

G

R

L

S

T

I

I

V

L

P

K

E

D

A

I

E

K

N

E

S

P

R

N

D

D

binding magnesium ion: D15 (= D13), D17 (= D15), D175 (= D173)

Sites not aligning to the query:

binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 250, 251, 253, 254, 279, 280, 334, 335, 336, 339, 369, 370

7ocnA Crystal structure of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
24% identity, 88% coverage: 5:199/222 of query aligns to 7:201/690 of 7ocnA

query
sites
7ocnA

R

K

Q

P

I

V

H

H

A

G

A

A

I

I

F

F

D
|
D

M

M

D
|
D

G

G

L

T

L

M

I

F

D

D

S

T

E

E

P

R

L

L

-

R

W

F

D

Q

K

T

A

L

E

Q

L

Q

E

A

V

S

M

Q

A

E

S

L

L

I

G

G

V

Q

D

E

I

F

S

S

R

H

R

E

H

Y

E

L

M

M

P

-

D

Q

I

C

L

L

G

G

L

L

R

S

I

A

-

T

-

A

-

E

D

K

L

L

V

A

V

Q

D

R

L

L

W

Y

F

G

A

V

Q

D

Q

V

P

P

W

Y

K

K

G

-

P

-

D

-

R

-

A

-

E

E

V

I

T

R

A

K

R

R

I

A

I

D

N

E

R

M

A

E

I

L

Q

E

L

H

V

I

E

R

E

K

-

H

A

G

R

V

P

P

L

I

L

K

P

K

G

G

A

L

R

V

Q

Q

A

V

V

L

A

E

L

R

C

L

K

R

A

K

Q

S

G

G

L

L

K

R

I

M

G

A

L

V

A

A

S

T

A

S

S

S

P

R

L

R

R

A

M

I

L

A

E

E

K

E

V

Y

L

L

T

I

M

N

F

A

E

N

L

V

R

Y

D

K

Q

F

F

F

D

D

A

V

L

I

A

T

S

C

A

G

E

D

M

E

L

V

P

E

F

Q

S

G

K

K

P

P

H

H

P

P

Q

E

V

I

Y

F

L

L

N

K

C

A

A

A

A

S

S

Q

L

L

G

H

V

L

S

D

P

A

M

N

N

Q

C

C

V

L

A

M

L

F

E

E

D
|
D

S

S

V

E

N

N

G

G

M

L

I

T

A

S

S

A

K

H

A

T

A

S

R

K

M

G

R

L

S

T

I

I

V

L

P

K

E

D

A

I

E

K

N

E

S

P

R

N

D

D

binding magnesium ion: D15 (= D13), D17 (= D15), D175 (= D173)

P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
27% identity, 94% coverage: 7:215/222 of query aligns to 2:212/221 of P71447

query
sites
P71447

I

F

H

K

A

A

A

V

I

L

F

F

D
|
D

M

L

D
|
D

G

G

L

V

L

I

I

T

D

D

S
x
T

E

A

P

E

L

Y

W
x
H

D

F

K

R

A

A

E

W

L

K

E

A

V

L

M

A

A

E

S

E

L

I

G

G

V

I

D

N

I

G

S

V

R

D

R

R

H

Q

E

F

M

N

P

E

D

Q

I

L

L
x
K

G
|
G

L

V

R

S

-
x
R

-

E

-

D

-
x
S

I

L

D

Q

L

K

V

I

V

L

D

D

L

L

W

-

F

-

A

A

Q

D

Q

K

P

K

W

V

K

S

G

A

P

E

D

E

R

F

A

K

E

E

V

L

T

A

A

K

R

R

I
x
K

I

N

N

D

R

N

A

Y

I

V

Q

K

L

M

V

I

E

Q

E

D

A

V

R

S

P

P

-

A

-

D

L

V

L

Y

P

P

G

G

A

I

R

L

Q

Q

A

L

V

L

A

K

L

D

C

L

K

R

A

S

Q

N

G

K

L

I

K

K

I

I

G

A

L

L

A

A

S

S

A

A

S

S

-

K

-

N

-

G

P

P

L

F

R

-

M

L

L

L

E

E

K

K

V

M

L

-

T

-

M

-

F

-

E

N

L

L

R

T

D

G

Q

Y

F

F

D

D

A

A

L

I

A

A

S

D

A

P

E

A

M

E

L

V

P

A

F

A

S

S

K

K

P

P

H

A

P

P

Q

D

V

I

Y

F

L

I

N

A

C

A

A

A

A

H

S

A

L

V

G

G

V

V

S

A

P

P

M

S

N

E

C

S

V

I

A

G

L

L

E

E

D
|
D

S

S

V

Q

N

A

G

G

M

I

I

Q

A

A

S

I

K

K

A

D

A

S

R

G

M

A

R

L

S

P

I

I

V

G

V

V

P

G

E

R

A

P

E

E

N

D

S

L

R

G

D

D

P

D

R

I

F

V

V

I

L

V

A

P

D

D

V

T

K

S

L

Y

A

Y

T

T

L

L

E

E

S

F

L

L

D8 (= D13) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
D10 (= D15) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
T16 (≠ S21) mutation to P: 500-fold reduction in the rate constant for Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold reduction in the apparent rate constant for cycling of the phosphorylated enzyme to convert beta-G1P to G6P. 13-fold increase in the estimated rate constant for phosphoryl transfer from the phospho-Asp8 to water.
H20 (≠ W25) mutation to A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P.; mutation to N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.; mutation to Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
K45 (≠ L50) mutation to A: 20'000-fold decrease in kcat/KM.
G46 (= G51) mutation to A: 1'000'000-fold decrease in kcat/KM.; mutation to P: 100'000-fold decrease in kcat/KM.; mutation to V: 10'000-fold decrease in kcat/KM.
R49 (vs. gap) mutation to K: 1'000'000-fold decrease in kcat/KM.
S52 (vs. gap) mutation to A: Wild-type activity.
K76 (≠ I79) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
D170 (= D173) mutation to A: Impaired, but active with an increase in the affinity for G1P.

4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
26% identity, 94% coverage: 7:215/222 of query aligns to 2:209/215 of 4c4sA

query
sites
4c4sA

I

F

H

K

A

A

A

V

I

L

F

F

D
|
D

M
x
L

D
|
D

G

G

L

V

L

I

I

T

D

D

S
x
T

E

A

P

E

L

Y

W
x
H

D

F

K

R

A

A

E
x
W

L

K

E

A

V

L

M

A

A

E

S

E

L

I

G

G

V

I

D

N

I

G

S

V

R

D

R

R

H

Q

E

F

M

N

P

E

D

Q

I
x
L

L
x
K

G
|
G

L
x
V

R

S

-
x
R

-

E

-

D

-

S

I

L

D

Q

L

K

V

I

V

L

D

D

L

L

W

K

F

V

A

S

Q

A

Q

E

P

E

W

F

K

K

G

-

P

-

D

-

R

-

A

-

E

E

V

L

T

A

A

K

R

R

I

K

I

N

N

D

R

N

A

Y

I

V

Q

K

L

M

V

I

E

Q

E

D

A

V

R

S

P

P

-

A

-

D

L

V

L

Y

P

P

G

G

A

I

R

L

Q

Q

A

L

V

L

A

K

L

D

C

L

K

R

A

S

Q

N

G

K

L

I

K

K

I

I

G

A

L

L

A

A

S
|
S

A
|
A

S
|
S

P

-

L

-

R

K

M

N

L

G

E

P

K

F

V

L

L

L

T

E

M

R

F

M

E

N

L

L

R

T

D

G

Q

Y

F

F

D

D

A

A

L

I

A

A

S

D

A

P

E

A

M

E

L

V

P

A

F

A

S

S

K
|
K

P

P

H

A

P

P

Q

D

V

I

Y

F

L

I

N

A

C

A

A

A

A

H

S

A

L

V

G

G

V

V

S

A

P

P

M

S

N

E

C

S

V

I

A

G

L

L

E
|
E

D
|
D

S

S

V

Q

N

A

G

G

M

I

I

Q

A

A

S

I

K

K

A

D

A

S

R

G

M

A

R

L

S

P

I

I

V

G

V

V

P

G

E

R

A

P

E

E

N

D

S

L

R

G

D

D

P

D

R

I

F

V

V

I

L

V

A

P

D

D

V

T

K

S

L

H

A

Y

T

T

L

L

E

E

S

F

L

L

active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S111 (= S115), A112 (= A116), K142 (= K148), E166 (= E172), D167 (= D173)
binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D15), H20 (≠ W25), W24 (≠ E29), L44 (≠ I49), G46 (= G51), V47 (≠ L52), R49 (vs. gap), S113 (= S117)
binding magnesium ion: D8 (= D13), D10 (= D15), D167 (= D173)
binding trifluoromagnesate: D8 (= D13), L9 (≠ M14), D10 (= D15), S111 (= S115), A112 (= A116), K142 (= K148)

5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
26% identity, 93% coverage: 9:215/222 of query aligns to 4:212/224 of 5olwA

query
sites
5olwA

A

A

A

V

I

L

F

F

D
|
D

M
x
L

D
|
D

G

G

L

V

L

I

I

T

D

D

S
x
T

E

A

P

E

L

Y

W

H

D

F

K

R

A

A

E

W

L

K

E

A

V

L

M

A

A

E

S

E

L

I

G

G

V

I

D

N

I

G

S

V

R

D

R

R

H

Q

E

F

M

N

P

E

D

Q

I

L

L
x
K

G

G

L

V

R

S

-

R

-

E

-

D

-

S

I

L

D

Q

L

K

V

I

V

L

D

D

L

L

W

-

F

-

A

A

Q

D

Q

K

P

K

W

V

K

S

G

A

P

E

D

E

R

F

A

K

E

E

V

L

T

A

A

K

R

R

I

K

I

N

N

D

R

N

A

Y

I

V

Q

K

L

M

V

I

E

Q

E

D

A

V

R

S

P
|
P

-

A

-

D

L
x
V

L

Y

P

P

G

G

A

I

R

L

Q

Q

A

L

V

L

A

K

L

D

C

L

K

R

A

S

Q

N

G

K

L

I

K

K

I

I

G

A

L

L

A

A

S
|
S

A
|
A

S

S

P

K

L

N

R

G

M

P

L

F

E

-

K

-

V

L

L

L

T
x
E

M

R

F

M

E
x
N

L

L

R

T

D

G

Q

Y

F

F

D

D

A

A

L

I

A

A

S

D

A

P

E

A

M

E

L

V

P

A

F

A

S

S

K
|
K

P

P

H

A

P

P

Q

D

V

I

Y

F

L

I

N

A

C

A

A

A

A

H

S

A

L

V

G

G

V

V

S

A

P

P

M

S

N

E

C

S

V

I

A

G

L

L

E
|
E

D
|
D

S
|
S

V

Q

N

A

G

G

M

I

I

Q

A

A

S

I

K

K

A

D

A

S

R

G

M

A

R

L

S

P

I

I

V

G

V

V

P

G

E

R

A

P

E

E

N

D

S

L

R

G

D

D

P

D

R

I

F

V

V

I

L

V

A

P

D

D

V

T

K

S

L

H

A

Y

T

T

L

L

E

E

S

F

L

L

active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S114 (= S115), A115 (= A116), K145 (= K148), E169 (= E172), D170 (= D173)
binding calcium ion: D8 (= D13), D10 (= D15), P89 (= P92), V92 (≠ L93), E124 (≠ T127), N127 (≠ E130), E169 (= E172), D170 (= D173), S171 (= S174)

6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/219 of 6qzgA

query
sites
6qzgA

I

F

H

K

A

A

A

V

I

L

F

F

D
|
D

M
x
L

D
|
D

G

G

L

V

L

I

I

T

D

D

S

T

E

A

P

E

L

Y

W
x
H

D

F

K

R

A

A

E

W

L

K

E

A

V

L

M

A

A

E

S

E

L

I

G

G

V

I

D

N

I

G

S

V

R

D

R

R

H

Q

E

F

M

N

P

E

D

Q

I

L

L

K

G
|
G

L

V

R

S

-

R

-

E

-

D

-

S

I

L

D

Q

L

K

V

I

V

L

D

D

L

L

W

-

F

-

A

A

Q

D

Q

K

P

K

W

V

K

S

G

A

P

E

D

E

R

F

A

K

E

E

V

L

T

A

A

K

R

R

I

K

I

N

N

D

R

N

A

Y

I

V

Q

K

L

M

V

I

E

Q

E

D

A

V

R

S

P

P

-

A

-

D

L

V

L

Y

P

P

G

G

A

I

R

L

Q

Q

A

L

V

L

A

K

L

D

C

L

K

R

A

S

Q

N

G

K

L

I

K

K

I

I

G

A

L

L

A

A

S
|
S

A
|
A

S
|
S

P
x
K

L

N

R

G

M

P

L

F

E

-

K

-

V

L

L

L

T

E

M

R

F

M

E

N

L

L

R

T

D

G

Q

Y

F

F

D

D

A

A

L

I

A

A

S

D

A

P

E

A

M

E

L

V

P

A

F

A

S

S

K
|
K

P

P

H

A

P

P

Q

D

V

I

Y

F

L

I

N

A

C

A

A

A

A

H

S

A

L

V

G

G

V

V

S

A

P

P

M

S

N

E

C

S

V

I

A

G

L

L

E

E

D
|
D

S

S

V

Q

N

A

G

G

M

I

I

Q

A

A

S

I

K

K

A

D

A

S

R

G

M

A

R

L

S

P

I

I

V

G

V

V

P

G

E

R

A

P

E

E

N

D

S

L

R

G

D

D

P

D

R

I

F

V

V

I

L

V

A

P

D

D

V

T

K

S

L

H

A

Y

T

T

L

L

E

E

S

F

L

L

binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D13), L9 (≠ M14), D10 (= D15), H20 (≠ W25), G46 (= G51), S114 (= S115), A115 (= A116), S116 (= S117), K117 (≠ P118), K145 (= K148)
binding magnesium ion: D8 (= D13), D10 (= D15), D170 (= D173)

1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/219 of 1z4nA

query
sites
1z4nA

I

F

H

K

A

A

A

V

I

L

F

F

D
|
D

M
x
L

D
|
D

G

G

L

V

L

I

I

T

D

D

S
x
T

E

A

P

E

L

Y

W
x
H

D

F

K

R

A

A

E
x
W

L

K

E

A

V

L

M

A

A

E

S

E

L

I

G

G

V

I

D

N

I

G

S

V

R

D

R

R

H

Q

E

F

M

N

P

E

D

Q

I

L

L
x
K

G

G

L
x
V

R

S

-
x
R

-

E

-

D

-

S

I

L

D

Q

L

K

V

I

V

L

D

D

L

L

W

-

F

-

A

A

Q

D

Q

K

P

K

W

V

K

S

G

A

P

E

D

E

R

F

A

K

E

E

V

L

T

A

A

K

R

R

I

K

I

N

N

D

R

N

A

Y

I

V

Q

K

L

M

V

I

E

Q

E

D

A

V

R

S

P

P

-

A

-

D

L

V

L

Y

P

P

G

G

A

I

R

L

Q

Q

A

L

V

L

A

K

L

D

C

L

K

R

A

S

Q

N

G

K

L

I

K

K

I

I

G

A

L

L

A

A

S
|
S

A
|
A

S
|
S

P
x
K

L
x
N

R

G

M

P

L

F

E

-

K

-

V

L

L

L

T

E

M

R

F

M

E

N

L

L

R

T

D

G

Q

Y

F

F

D

D

A

A

L

I

A

A

S

D

A

P

E

A

M

E

L

V

P

A

F

A

S

S

K
|
K

P

P

H

A

P

P

Q

D

V

I

Y

F

L

I

N

A

C

A

A

A

A

H

S

A

L

V

G

G

V

V

S

A

P

P

M

S

N

E

C

S

V

I

A

G

L

L

E
|
E

D
|
D

S

S

V

Q

N

A

G

G

M

I

I

Q

A

A

S

I

K

K

A

D

A

S

R

G

M

A

R

L

S

P

I

I

V

G

V

V

P

G

E

R

A

P

E

E

N

D

S

L

R

G

D

D

P

D

R

I

F

V

V

I

L

V

A

P

D

D

V

T

K

S

L

H

A

Y

T

T

L

L

E

E

S

F

L

L

active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S114 (= S115), A115 (= A116), K145 (= K148), E169 (= E172), D170 (= D173)
binding 1-O-phosphono-alpha-D-galactopyranose: H20 (≠ W25), W24 (≠ E29), V47 (≠ L52), R49 (vs. gap), S116 (= S117), K117 (≠ P118), N118 (≠ L119)
binding magnesium ion: D8 (= D13), D10 (= D15), E169 (= E172), D170 (= D173)

6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/218 of 6h91A

query
sites
6h91A

I

F

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K

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A

A

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M

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R

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D

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-

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-

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A

P

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D

E

R

F

A

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E

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I

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N

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-

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A

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L

binding magnesium ion: D8 (= D13), D10 (= D15), D170 (= D173)
binding acetylphosphate: R49 (vs. gap), K117 (≠ R120)

4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/218 of 4c4rA

query
sites
4c4rA

I

F

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x
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D

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E

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x
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x
K

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G

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-
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R

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x
S

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D

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N

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D

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active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S114 (= S115), A115 (= A116), K145 (= K148), E169 (= E172), D170 (= D173)
binding magnesium ion: D8 (= D13), D10 (= D15), D170 (= D173)
binding trifluoromagnesate: D8 (= D13), L9 (≠ M14), D10 (= D15), S114 (= S115), A115 (= A116), K145 (= K148)
binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D15), H20 (≠ W25), W24 (≠ E29), L44 (≠ I49), G46 (= G51), V47 (≠ L52), R49 (vs. gap), S52 (vs. gap), S116 (= S117), K117 (≠ R120)

3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/218 of 3zi4A

query
sites
3zi4A

I

F

H

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S

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S

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K

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A

A

A

A

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A

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K

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active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S114 (= S115), A115 (= A116), K145 (= K148), E169 (= E172), D170 (= D173)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D15), H20 (≠ W25), G46 (= G51), V47 (≠ L52), R49 (vs. gap), S116 (= S117), K117 (≠ R120)
binding magnesium ion: D8 (= D13), D10 (= D15), D170 (= D173)
binding Scandium Tetrafluoride: D8 (= D13), L9 (≠ M14), D10 (= D15), S114 (= S115), A115 (= A116), K145 (= K148)

2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
26% identity, 94% coverage: 7:215/222 of query aligns to 2:212/218 of 2wf8A

query
sites
2wf8A

I

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S

A
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A

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S

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K

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K

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C

A

A

A

A

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G

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D

S

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K

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D

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D

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H

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T

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L

L

E

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L

L

active site: D8 (= D13), L9 (≠ M14), D10 (= D15), T16 (≠ S21), K45 (≠ L50), S114 (= S115), A115 (= A116), K145 (= K148), E169 (= E172), D170 (= D173)
binding beryllium trifluoride ion: D8 (= D13), L9 (≠ M14), D10 (= D15), S114 (= S115), A115 (= A116), K145 (= K148)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D15), H20 (≠ W25), G46 (= G51), V47 (≠ L52), R49 (vs. gap), A115 (= A116), S116 (= S117), K117 (≠ R120)
binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D15), H20 (≠ W25), W24 (≠ E29), L44 (≠ I49), G46 (= G51), V47 (≠ L52), R49 (vs. gap), S52 (vs. gap), A115 (= A116), S116 (= S117), K117 (≠ R120)
binding magnesium ion: D8 (= D13), D10 (= D15), D170 (= D173)

Query Sequence

>BWI76_RS11780 FitnessBrowser__Koxy:BWI76_RS11780
MSARRQIHAAIFDMDGLLIDSEPLWDKAELEVMASLGVDISRRHEMPDILGLRIDLVVDL
WFAQQPWKGPDRAEVTARIINRAIQLVEEARPLLPGARQAVALCKAQGLKIGLASASPLR
MLEKVLTMFELRDQFDALASAEMLPFSKPHPQVYLNCAASLGVSPMNCVALEDSVNGMIA
SKAARMRSIVVPEAENSRDPRFVLADVKLATLESLTPGDLLG

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