SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing HSERO_RS00780 FitnessBrowser__HerbieS:HSERO_RS00780 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)

2fdrA Crystal structure of conserved haloacid dehalogenase-like protein of unknown function atu0790 from agrobacterium tumefaciens str. C58
35% identity, 83% coverage: 10:188/215 of query aligns to 4:184/222 of 2fdrA

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binding magnesium ion: D8 (= D14), D10 (= D16), D166 (= D170)

4eenA Crystal structure of had family hydrolase dr_1622 from deinococcus radiodurans r1 (target efi-501256) with bound magnesium
34% identity, 75% coverage: 11:172/215 of query aligns to 7:171/229 of 4eenA

query
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4eenA

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active site: D10 (= D14), D12 (= D16), V16 (= V20), S18 (= S22), M44 (≠ A48), Y45 (≠ R49), T47 (≠ R51), S109 (= S111), N110 (= N112), K144 (= K145), E168 (= E169), D169 (= D170)
binding magnesium ion: D10 (= D14), D12 (= D16), D169 (= D170)

Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 83% coverage: 11:189/215 of query aligns to 77:261/1055 of Q8VZ10

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D80 (= D14) 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.

6w04A Crystal structure of had hydrolase, family ia, variant 3 from entamoeba histolytica hm-1:imss
24% identity, 80% coverage: 11:182/215 of query aligns to 4:181/223 of 6w04A

query
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active site: D7 (= D14), F8 (≠ C15), N9 (≠ D16), D15 (≠ S22), N44 (≠ R51), T109 (≠ S111), S110 (≠ N112), K144 (= K145), E168 (= E169), D169 (= D170)
binding magnesium ion: D7 (= D14), N9 (≠ D16), D169 (= D170)

1te2A Putative phosphatase ynic from escherichia coli k12
29% identity, 82% coverage: 12:188/215 of query aligns to 7:187/218 of 1te2A

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active site: D9 (= D14), D11 (= D16), S17 (= S22), D44 (≠ R49), S111 (= S111), A112 (≠ N112), K144 (= K145), E168 (= E169), D169 (= D170)
binding calcium ion: D9 (= D14), D11 (= D16), D169 (= D170)
binding 2-phosphoglycolic acid: D9 (= D14), M10 (≠ C15), D11 (= D16), G47 (= G52), S111 (= S111), A112 (≠ N112), K144 (= K145)

4uavA Crystal structure of cbby (at3g48420) from arabidobsis thaliana (see paper)
30% identity, 95% coverage: 6:209/215 of query aligns to 1:225/246 of 4uavA

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binding magnesium ion: D9 (= D14), D11 (= D16), D185 (= D170)

Q94K71 CBBY-like protein; AtCbby; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 97% coverage: 2:209/215 of query aligns to 70:298/319 of Q94K71

query
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Q94K71

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E

-

R

-

D

-

L

-

N

-

V

A

T

W

W

S

D

E

-

Y

-

V

V

A

D

T

L

Y
|
Y

G

G

V

E

Q

L

L

L

T

K

-

I

-

G

P

K

E

E

D
x
R

A

M

L

T

A

A

R

Y

F

F

R

N

G

K

V

V

S

G

M

W

S

P

W

E

C

K

I

A

A

P

H

K

V

D

A

E

Q

A

L

E

R

R

G

K

Q

E

A

F

L

I

P

A

A

G

H

L

F

H

E

K

Q

Q

E
x
K

L

T

R

E

A

L

R

F

M

M

G

-

V

V

M

L

L

I

E

E

Q

K

H

K

L

L

Q

L

P

P

I

L

N

R

-

P

G

G

A

V

L

A

E

K

M

L

V

V

E

D

Q

Q

-

A

L

L

Q

T

I

N

P

G

F

V

A

K

L

V

A

A

S

V

N

C

A

S

P

T

H

S

H

N

K

E

I

K

E

A

L

V

C

S

L

A

R

I

V

V

T

S

G

C

L

L

P

G

H

P

F

E

H

R

G

A

-

E

-

K

-

I

R

K

I

I

F

F

S

A

A

G

Y

D

D

V

V

V

Q

P

R

K

W

K

K

K

P

P

D

D

P

P

A

A

L

I

F

Y

L

N

F

L

A

A

E

E

R

T

L

L

G

G

V

V

P

D

P

P

A

S

R

K

C

C

A

V

V

V

E

E

D

D

S

S

L

A

P

I

G

G

V

L

Q

A

A

A

G

A

L

K

A

A

G

G

M

M

K

T

V

C

I

I

A

V

L

T

Q

K

E

S

-

G

H

Y

G

T

V

A

H

D

P

E

D

D

L

F

P

E

E

N

E

A

V

D

A

A

V

V

I

F

T

D

H

C

L

I

G

G

Q

D

D84 (= D16) mutation to N: Loss of catalytic activity.
E91 (= E23) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
H95 (≠ A27) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
Y117 (= Y37) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
R129 (≠ D45) mutation to A: 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
K161 (≠ E77) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.

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)
29% identity, 82% coverage: 12:188/215 of query aligns to 11:191/222 of P77247

query
sites
P77247

I

I

F

F

D
|
D

C

M

D
|
D

G

G

T

L

L

L

V

I

D

D

S

S

E

E

V

P

V

L

A

W

A

D

R

R

A

A

W

E

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L

E

D

Y

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V

M

A

A

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Y

L

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G

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V

Q

D

L

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P

R

E

R

D

N

A

E

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L

A

P

R

D

F

T

R

L

G

G

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M

I

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M

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I

V

A

D

H

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A

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A

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R

Q

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P

Q

W

A

N

L

G

P

P

A

S

H

R

F

Q

E

E

-

V

Q

E

E

R

L

V

R

I

A

A

R

R

M

A

G

I

V

S

M

L

L

V

E

E

Q

E

H

T

-

R

-

P

-

L

L

L

Q

P

P

G

I

V

N

R

G

E

A

A

L

V

E

A

M

L

V

C

E

K

Q

E

L

Q

Q

G

I

L

P

L

F

V

A

G

L

L

A

A

S

S

N

A

A

S

P

P

H

L

H

H

K

M

I

L

E

E

L

K

C

V

L

L

R

T

V

M

T

F

G

D

L

L

L

R

P

D

H

S

F

F

H

D

G

A

R

-

I

L

F

A

S

S

A

A

Y

E

D

K

V

L

Q

P

R

Y

W

S

K

K

P

P

D

H

P

P

A

Q

L

V

F

Y

L

L

F

D

A

C

A

A

E

A

R

K

L

L

G

G

V

V

P

D

P

P

A

L

R

T

C

C

A

V

V

A

V

L

E

E

D
|
D

S

S

L

V

P

N

G

G

V

M

Q

I

A

A

G

S

L

K

A

A

G

R

M

M

K

R

V

S

I

I

A

V

L

V

D13 (= D14) binding ; mutation to A: Loss of phosphatase activity.
D15 (= D16) binding
D173 (= D170) binding

4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
29% identity, 83% coverage: 11:188/215 of query aligns to 7:191/227 of 4g9bA

query
sites
4g9bA

V

V

I

I

F

F

D
|
D

C
x
L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

H

V

L

A

H

A

F

R

Q

A

A

W

W

S

Q

E

Q

Y

I

V

A

A

A

T

E

Y

I

G

G

V

I

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L

I

T

D

P

A

E

Q

D

F

A

N

L

-

A

E

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F

L

R
x
K

G

G

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S

M

R

S

D

W

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I

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A

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R

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I

A

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Q

L

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A

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L

-

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E

A

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F

F

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E

Q

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E

R

R

A

A

-

Q

-

L

-

A

-

Y

R

R

M

K

G

N

V

L

M

L

L

Y

E

V

Q

H

H

S

L

L

Q

R

-

E

-

L

P

T

I

V

N

N

G

A

A

V

L

L

E

P

M

G

V

I

E

R

Q

S

L

L

-

L

-

A

-

D

-

L

-

R

-

A

-

Q

Q

Q

I

I

P

S

F

V

A

G

L

L

A

A

S
|
S

-
x
V

-

S

-

L

N

N

A

A

P

P

H

T

H

I

K

L

I

A

E

A

L

L

C

E

L

L

R

R

V

-

T

-

G

-

L

-

P

-

H

E

F

F

H

F

G

T

R

F

I

C

F

A

S

D

A

A

Y

S

D

Q

V

L

Q

K

R

N

W

S

K
|
K

P

P

D

D

P

P

A

E

L

I

F

F

L

L

F

A

A

A

A

C

E

A

R

G

L

L

G

G

V

V

P

P

A

Q

R

A

C

C

A

I

V

G

V

I

E
|
E

D
|
D

S

A

L

Q

P

A

G

G

V

I

Q

D

A

A

G

I

L

N

A

A

A

S

G

G

M

M

K

R

V

S

I

V

A

G

L

I

active site: D10 (= D14), L11 (≠ C15), D12 (= D16), T18 (≠ S22), K46 (≠ R51), S117 (= S111), V118 (vs. gap), K148 (= K145), E172 (= E169), D173 (= D170)
binding magnesium ion: D10 (= D14), D12 (= D16), D173 (= D170)

3dv9A Putative beta-phosphoglucomutase from bacteroides vulgatus.
28% identity, 87% coverage: 11:197/215 of query aligns to 26:214/243 of 3dv9A

query
sites
3dv9A

V

V

I

L

F

F

D
|
D

C
x
M

D
|
D

G

G

T

V

L

L

V

F

D

D

S
|
S

E

M

V

P

V

N

A

H

A

A

R

E

A

S

W

W

S

H

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Y

I

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M

A

K

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Y

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G

V

F

Q

G

L

L

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P

R

E

E

D

E

A

A

L

Y

A

M

R

H

F

-

R
x
E

G

G

V

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S

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M

G

S

A

W

S

C

T

I

I

A

N

H

I

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V

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S

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R

-

E

R

R

G

G

Q

H

A

D

L

A

P

T

A

-

H

-

F

-

E

E

Q

E

E

E

L

I

R

K

A

A

R

I

M

Y

G

Q

V

A

M

K

L

T

E

E

Q

E

-

F

-

N

-

K

-

C

-

P

H

K

L

A

Q

E

P

R

I

M

N

P

G

G

A

A

L

L

E

E

M

V

V

L

E

T

Q

K

L

I

Q

K

-

S

-

E

-

G

-

L

I

T

P

P

F

M

A

V

L

V

A
x
T

S
x
G

N

S

A

G

P

-

H

-

K

-

I

-

E

-

L

L

C

L

L

D

R

R

V

L

T

N

G

H

L

N

L

F

P

P

H

G

-

I

F

F

H

Q

G

A

R

N

I

L

F

M

-

V

S

T

A

A

Y

F

D

D

V

V

Q

K

R

Y

W

G

K
|
K

P

P

D

N

P

P

A

E

L

P

F

Y

L

L

F

M

A

A

A

L

E

K

R

K

L

G

G

G

V

F

P

K

P

P

A

N

R

E

C

A

A

L

V

V

V

I

E
|
E

D
x
N

S

A

L

P

P

L

G

G

V

V

Q

Q

A

A

G

G

L

V

A

A

G

G

M

I

K

F

V

T

I

I

A

A

L

V

Q

N

E

T

H

G

G

P

V

L

H

H

P

D

D

N

L

V

active site: D29 (= D14), M30 (≠ C15), D31 (= D16), S37 (= S22), E65 (≠ R51), T131 (≠ A110), G132 (≠ S111), K162 (= K145), E186 (= E169), N187 (≠ D170)
binding magnesium ion: D29 (= D14), D31 (= D16), E65 (≠ R51), N187 (≠ D170)

4ex7A Crystal structure of the alnumycin p phosphatase in complex with free phosphate (see paper)
28% identity, 87% coverage: 11:196/215 of query aligns to 4:193/217 of 4ex7A

query
sites
4ex7A

V

V

I

I

F

L

D
|
D

C
x
L

D
|
D

G

G

T

T

L

L

V

A

D

D

S

T

E

P

V

A

A

I

A

A

R

T

A

I

W

T

S

A

E

E

Y

V

V

L

A

A

T

A

Y

M

G

G

V

T

Q

A

L

V

T

S

P

-

E

-

D

-

A

-

L

-

A

-

R

-

F

-

R

R

G

G

V

A

S

I

M

L

S

S

W

T

C

V

I
x
G

-

R

-

P

-

L

-

P

A

A

H

S

V

L

A

A

Q

G

L

L

R

L

G

G

Q

V

A

P

L

V

P

E

A

D

H

P

F

R

E

V

Q

A

E

E

L

A

R

T

A

E

R

E

M

Y

G

G

V

R

M

R

L

F

E

G

Q

A

H

H

L

V

Q

R

P

A

I

A

N

G

-

P

-

R

-

L

-

Y

-

P

G

G

A

V

L

L

E

E

M

G

V

L

E

D

Q

R

L

L

Q

S

I

A

P

A

-

G

-

F

-

R

F

L

A

A

L

M

A

A

S
x
T

N
x
S

A

K

P

V

H

E

H

K

K

A

I

A

E

R

L

A

C

I

L

A

R

E

V

L

T

T

G

G

L

L

L

D

P

T

H

R

F

L

H

T

G

-

R

-

I

V

F

I

S

A

A

G

Y

D

D

D

-

S

V

V

Q

E

R

R

W

G

K

K

P

P

D

H

P

P

A

D

L

M

F

A

L

L

F

H

A

V

A

A

E

R

R

G

L

L

G

G

V

I

P

P

A

E

R

R

C

C

A

V

V

V

V

I

E

G

D
|
D

S

G

L

V

P

P

G

D

V

A

Q

E

A

M

G

G

L

R

A

A

G

G

M

M

K

T

V

V

I

I

A

G

L

V

Q

S

E

Y

H

G

G

V

V

S

H

G

P

P

D

D

binding magnesium ion: D7 (= D14), D9 (= D16), D167 (= D170)
binding phosphate ion: D7 (= D14), L8 (≠ C15), D9 (= D16), G44 (≠ I59), T109 (≠ S111), S110 (≠ N112)

4ex6A Crystal structure of the alnumycin p phosphatase alnb (see paper)
28% identity, 87% coverage: 11:196/215 of query aligns to 6:195/219 of 4ex6A

query
sites
4ex6A

V

V

I

I

F

L

D
|
D

C

L

D
|
D

G

G

T

T

L

L

V

A

D

D

S

T

E

P

V

A

A

I

A

A

R

T

A

I

W

T

S

A

E

E

Y

V

V

L

A

A

T

A

Y

M

G

G

V

T

Q

A

L

V

T

S

P

-

E

-

D

-

A

-

L

-

A

-

R

-

F

-

R

R

G

G

V

A

S

I

M

L

S

S

W

T

C

V

I

G

-

R

-

P

-

L

-

P

A

A

H

S

V

L

A

A

Q

G

L

L

R

L

G

G

Q

V

A

P

L

V

P

E

A

D

H

P

F

R

E

V

Q

A

E

E

L

A

R

T

A

E

R

E

M

Y

G

G

V

R

M

R

L

F

E

G

Q

A

H

H

L

V

Q

R

P

A

I

A

N

G

-

P

-

R

-

L

-

Y

-

P

G

G

A

V

L

L

E

E

M

G

V

L

E

D

Q

R

L

L

Q

S

I

A

P

A

-

G

-

F

-

R

F

L

A

A

L

M

A

A

S

T

N

S

A

K

P

V

H

E

H

K

K

A

I

A

E

R

L

A

C

I

L

A

R

E

V

L

T

T

G

G

L

L

L

D

P

T

H

R

F

L

H

T

G

-

R

-

I

V

F

I

S

A

A

G

Y

D

D

D

-

S

V

V

Q

E

R

R

W

G

K

K

P

P

D

H

P

P

A

D

L

M

F

A

L

L

F

H

A

V

A

A

E

R

R

G

L

L

G

G

V

I

P

P

A

E

R

R

C

C

A

V

V

V

V

I

E

G

D
|
D

S

G

L

V

P

P

G

D

V

A

Q

E

A

M

G

G

L

R

A

A

G

G

M

M

K

T

V

V

I

I

A

G

L

V

Q

S

E

Y

H

G

G

V

V

S

H

G

P

P

D

D

binding magnesium ion: D9 (= D14), D11 (= D16), D169 (= D170)

5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/224 of 5olwA

query
sites
5olwA

V

V

I

L

F

F

D
|
D

C
x
L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

E

V

Y

A

H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R
x
K

G

G

V

V

S

S

M

R

S

E

W

D

C

S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

V

P

S

A

A

H

E

F

E

E

F

Q

K

E

E

L

L

R

A

A

K

R

R

M

K

G

N

-

D

-

N

-

Y

V

V

M

K

L

M

E

I

Q

Q

H

D

L

V

Q

S

P
|
P

I

A

N

D

-
x
V

-

Y

-

P

G

G

A

I

L

L

E

Q

M

L

V

L

E

K

Q

D

L

L

-

R

-

S

-

N

Q

K

I

I

P

K

F

I

A

A

L

L

A

A

S
|
S

-
x
A

-

S

-

K

N

N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R
x
E

V

R

T

M

G
x
N

L

L

L

T

P

G

H

Y

F

F

H

D

G

A

R

-

I

I

F

A

S

D

A

P

Y

A

D

E

V

V

Q

A

R

A

W

S

K
|
K

P

P

D

A

P

P

A

D

L

I

F

F

L

I

F

A

A

A

E

H

R

A

L

V

G

G

V

V

P

A

P

P

A

S

R

E

C

S

A

I

V

G

V

L

E
|
E

D
|
D

S
|
S

L

Q

P

A

G

G

V

I

Q

Q

A

A

G

I

L

K

A

D

A

S

G

G

M

A

K

L

V

P

I

I

A

G

L

V

Q

-

E

-

H

-

G

G

V

R

H

P

P

E

D

D

L

L

P

G

E

D

V

I

A

V

V

I

I

V

active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding calcium ion: D8 (= D14), D10 (= D16), P89 (= P92), V92 (vs. gap), E124 (≠ R123), N127 (≠ G126), E169 (= E169), D170 (= D170), S171 (= S171)

P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/221 of P71447

query
sites
P71447

V

V

I

L

F

F

D
|
D

C

L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

E

V

Y

A
x
H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R
x
K

G
|
G

V

V

S

S

M
x
R

S

E

W

D

C
x
S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

V

P

S

A

A

H

E

F

E

E

F

Q

K

E

E

L

L

R

A

A

K

R

R

M
x
K

G

N

-

D

-

N

-

Y

V

V

M

K

L

M

E

I

Q

Q

H

D

L

V

Q

S

P

P

I

A

N

D

-

V

-

Y

-

P

G

G

A

I

L

L

E

Q

M

L

V

L

E

K

Q

D

L

L

-

R

-

S

-

N

Q

K

I

I

P

K

F

I

A

A

L

L

A

A

S

S

-

A

-

S

-

K

N

N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R

E

V

K

T

M

G

N

L

L

L

T

P

G

H

Y

F

F

H

D

G

A

R

-

I

I

F

A

S

D

A

P

Y

A

D

E

V

V

Q

A

R

A

W

S

K

K

P

P

D

A

P

P

A

D

L

I

F

F

L

I

F

A

A

A

E

H

R

A

L

V

G

G

V

V

P

A

P

P

A

S

R

E

C

S

A

I

V

G

V

L

E

E

D
|
D

S

S

L

Q

P

A

G

G

V

I

Q

Q

A

A

G

I

L

K

A

D

A

S

G

G

M

A

K

L

V

P

I

I

A

G

L

V

Q

-

E

-

H

-

G

G

V

R

H

P

P

E

D

D

L

L

P

G

E

D

V

I

A

V

V

I

I

V

D8 (= D14) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
D10 (= D16) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
T16 (≠ S22) 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 (≠ A26) 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 (≠ R51) mutation to A: 20'000-fold decrease in kcat/KM.
G46 (= G52) 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 (≠ M55) mutation to K: 1'000'000-fold decrease in kcat/KM.
S52 (≠ C58) mutation to A: Wild-type activity.
K76 (≠ M82) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
D170 (= D170) mutation to A: Impaired, but active with an increase in the affinity for G1P.

2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/221 of 2wf9A

query
sites
2wf9A

V

V

I

L

F

F

D
|
D

C
x
L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

E

V

Y

A
x
H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R
x
K

G
|
G

V
|
V

S

S

M
x
R

S

E

W

D

C

S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

V

P

S

A

A

H

E

F

E

E

F

Q

K

E

E

L

L

R

A

A

K

R

R

M

K

G

N

-

D

-

N

-

Y

V

V

M

K

L

M

E

I

Q

Q

H

D

L

V

Q

S

P

P

I

A

N

D

-

V

-

Y

-

P

G

G

A

I

L

L

E

Q

M

L

V

L

E

K

Q

D

L

L

-

R

-

S

-

N

Q

K

I

I

P

K

F

I

A

A

L

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

N
|
N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R

E

V

R

T

M

G

N

L

L

L

T

P

G

H

Y

F

F

H

D

G

A

R

-

I

I

F

A

S

D

A

P

Y

A

D

E

V

V

Q

A

R

A

W

S

K
|
K

P

P

D

A

P

P

A

D

L

I

F

F

L

I

F

A

A

A

E

H

R

A

L

V

G

G

V

V

P

A

P

P

A

S

R

E

C

S

A

I

V

G

V

L

E
|
E

D
|
D

S

S

L

Q

P

A

G

G

V

I

Q

Q

A

A

G

I

L

K

A

D

A

S

G

G

M

A

K

L

V

P

I

I

A

G

L

V

Q

-

E

-

H

-

G

G

V

R

H

P

P

E

D

D

L

L

P

G

E

D

V

I

A

V

V

I

I

V

active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding beryllium trifluoride ion: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (vs. gap), K145 (= K145)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), H20 (≠ A26), G46 (= G52), V47 (= V53), R49 (≠ M55), S116 (vs. gap), K117 (vs. gap), N118 (= N112)
binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D16), H20 (≠ A26), G46 (= G52), V47 (= V53), R49 (≠ M55), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap), N118 (= N112)
binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)

1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/221 of 1o03A

query
sites
1o03A

V

V

I

L

F

F

D
|
D

C
x
L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

E

V

Y

A
x
H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R
x
K

G
|
G

V
|
V

S

S

M
x
R

S

E

W

D

C

S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

V

P

S

A

A

H

E

F

E

E

F

Q

K

E

E

L

L

R

A

A

K

R

R

M

K

G

N

-

D

-

N

-

Y

V

V

M

K

L

M

E

I

Q

Q

H

D

L

V

Q

S

P

P

I

A

N

D

-

V

-

Y

-

P

G

G

A

I

L

L

E

Q

M

L

V

L

E

K

Q

D

L

L

-

R

-

S

-

N

Q

K

I

I

P

K

F

I

A

A

L

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

N

N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R

E

V

R

T

M

G

N

L

L

L

T

P

G

H

Y

F

F

H

D

G

A

R

-

I

I

F

A

S

D

A

P

Y

A

D

E

V

V

Q

A

R

A

W

S

K
|
K

P

P

D

A

P

P

A

D

L

I

F

F

L

I

F

A

A

A

E

H

R

A

L

V

G

G

V

V

P

A

P

P

A

S

R

E

C

S

A

I

V

G

V

L

E
|
E

D
|
D

S

S

L

Q

P

A

G

G

V

I

Q

Q

A

A

G

I

L

K

A

D

A

S

G

G

M

A

K

L

V

P

I

I

A

G

L

V

Q

-

E

-

H

-

G

G

V

R

H

P

P

E

D

D

L

L

P

G

E

D

V

I

A

V

V

I

I

V

active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D14), L9 (≠ C15), D10 (= D16), H20 (≠ A26), G46 (= G52), V47 (= V53), R49 (≠ M55), S114 (= S111), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap), K145 (= K145)
binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)

1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/221 of 1lvhA

query
sites
1lvhA

V

V

I

L

F

F

D
|
D

C
x
L

D
|
D

G

G

T

V

L

I

V

T

D

D

S
x
T

E

A

V

E

V

Y

A

H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R
x
K

G

G

V

V

S

S

M

R

S

E

W

D

C

S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

V

P

S

A

A

H

E

F

E

E

F

Q

K

E

E

L

L

R

A

A

K

R

R

M

K

G

N

-

D

-

N

-

Y

V

V

M

K

L

M

E

I

Q

Q

H

D

L

V

Q

S

P

P

I

A

N

D

-

V

-

Y

-

P

G

G

A

I

L

L

E

Q

M

L

V

L

E

K

Q

D

L

L

-

R

-

S

-

N

Q

K

I

I

P

K

F

I

A

A

L

L

A

A

S
|
S

-
x
A

-

S

-

K

N

N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R

E

V

R

T

M

G

N

L

L

L

T

P

G

H

Y

F

F

H

D

G

A

R

-

I

I

F

A

S

D

A

P

Y

A

D

E

V

V

Q

A

R

A

W

S

K
|
K

P

P

D

A

P

P

A

D

L

I

F

F

L

I

F

A

A

A

E

H

R

A

L

V

G

G

V

V

P

A

P

P

A

S

R

E

C

S

A

I

V

G

V

L

E
|
E

D
|
D

S

S

L

Q

P

A

G

G

V

I

Q

Q

A

A

G

I

L

K

A

D

A

S

G

G

M

A

K

L

V

P

I

I

A

G

L

V

Q

-

E

-

H

-

G

G

V

R

H

P

P

E

D

D

L

L

P

G

E

D

V

I

A

V

V

I

I

V

active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)

6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/218 of 6h91A

query
sites
6h91A

V

V

I

L

F

F

D
|
D

C

L

D
|
D

G

G

T

V

L

I

V

T

D

D

S

T

E

A

V

E

V

Y

A

H

A

F

R

R

A

A

W

W

S

K

E

A

Y

L

V

A

A

E

T

E

Y

I

G

G

V

I

Q

N

L

G

T

V

P

D

E

R

D

Q

A

F

L

N

A

E

R

Q

F

L

R

K

G

G

V

V

S

S

M
x
R

S

E

W

D

C

S

I

L

A

Q

H

K

V

I

A

L

Q

D

L

L

R

A

G

D

Q

K

A

K

L

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H

E

F

E

E

F

Q

K

E

E

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N

-

D

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Y

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K

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D
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D

S

S

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A

D

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binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
binding acetylphosphate: R49 (≠ M55), K117 (vs. gap)

4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/218 of 4c4rA

query
sites
4c4rA

V

V

I

L

F

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D
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D

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x
L

D
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D

G

G

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E

A

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G

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A

E

R

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x
L

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x
K

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G

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V

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x
R

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x
S

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I

A

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A

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E

E

F

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E

E

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N

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M

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L

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K

F

I

A

A

L

L

A

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S
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S

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x
A

-
x
S

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x
K

N

N

A

G

P

P

H

-

K

-

I

-

E

-

L

F

C

L

L

L

R

E

V

R

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M

G

N

L

L

L

T

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G

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Y

F

F

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-

I

I

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K

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A

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G

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E

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D

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S

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A

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A

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K

A

D

A

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A

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I

A

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-

E

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H

-

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D

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active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
binding trifluoromagnesate: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (vs. gap), K145 (= K145)
binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D16), H20 (≠ A26), W24 (= W30), L44 (≠ F50), G46 (= G52), V47 (= V53), R49 (≠ M55), S52 (≠ C58), S116 (vs. gap), K117 (vs. gap)

3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
27% identity, 90% coverage: 11:204/215 of query aligns to 5:201/218 of 3zi4A

query
sites
3zi4A

V

V

I

L

F

F

D
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D

C
x
L

D
|
D

G

G

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x
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A
x
H

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W

W

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K

E

A

Y

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A

A

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E

Y

I

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G

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I

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K

G
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G

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V

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S

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x
R

S

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W

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C

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A

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H

K

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I

A

L

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L

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E

E

F

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A

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A

L

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S

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x
A

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x
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x
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H

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-

I

-

E

-

L

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L

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I

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K

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A

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A

A

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E

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D

S

S

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A

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G

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I

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Q

A

A

G

I

L

K

A

D

A

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G

G

M

A

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I

I

A

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E

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-

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E

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D

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active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ R51), S114 (= S111), A115 (vs. gap), K145 (= K145), E169 (= E169), D170 (= D170)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), H20 (≠ A26), G46 (= G52), V47 (= V53), R49 (≠ M55), S116 (vs. gap), K117 (vs. gap)
binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
binding Scandium Tetrafluoride: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (vs. gap), K145 (= K145)

Query Sequence

>HSERO_RS00780 FitnessBrowser__HerbieS:HSERO_RS00780
MNDFATSPALVIFDCDGTLVDSEVVAARAWSEYVATYGVQLTPEDALARFRGVSMSWCIA
HVAQLRGQALPAHFEQELRARMGVMLEQHLQPINGALEMVEQLQIPFALASNAPHHKIEL
CLRVTGLLPHFHGRIFSAYDVQRWKPDPALFLFAAERLGVPPARCAVVEDSLPGVQAGLA
AGMKVIALQEHGVHPDLPEEVAVITHLGQLHPHLA

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