SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3607123 FitnessBrowser__Dino:3607123 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
33% identity, 89% coverage: 21:239/246 of query aligns to 3:218/222 of 2fdrA

query
sites
2fdrA

D

D

L

L

V

I

I

I

F

F

D
|
D

F

C

D
|
D

G

G

V

V

I

L

A

V

D

D

S

S

E

E

V

I

I

I

S

A

L

A

A

Q

T

V

L

E

Q

S

A

R

S

L

L

L

K

T

A

E

F

A

G

G

M

Y

D

P

L

I

T

S

I

V

E

E

I

M

R

G

Q

E

K

R

F

F

L

A

G

G

K

M

S

T

L

W

K

K

T

N

I

I

S

L

T

L

Y

Q

V

V

D

E

Q

S

H

E

S

A

S

S

S

I

Q

P

A

L

A

S

A

A

D

S

F

L

G

L

N

D

A

K

W

S

Q

E

A

K

E

L

L

L

Y

D

S

M

R

R

F

L

R

E

A

R

E

D

L

V

K

K

P

I

L

I

P

-

H

-

L

-

E

D

K

G

L

V

L

K

F

F

E

A

L

L

A

S

E

R

T

L

A

T

T

T

R

P

F

R

C

C

I

I

A

C

S

S

S

N

G

S

T

S

F

S

E

H

R

R

I

L

N

D

V

M

A

M

L

L

S

T

A

K

M

V

S

G

M

L

S

K

D

P

C

Y

F

F

-

A

D

P

H

H

V

I

F

Y

S

S

S

A

E

K

Q

D

V

L

S

G

-

A

-

D

R

R

G

V

K

K

P

P

A

K

P

P

D

D

L

I

F

F

L

L

M

H

A

G

A

A

E

A

A

Q

L

F

D

G

V

V

S

S

P

P

S

D

R

R

C

V

L

V

V

V

I

V

E

E

D
|
D

S

S

L

V

Y

H

G

G

I

I

R

H

A

G

A

A

K

R

A

A

G

G

M

M

R

R

G

V

V

I

G

G

F

F

L

T

G

G

G

A

A

S

H

H

L

-

Q

-

G

-

I

T

V

Y

E

P

Q

S

H

H

G

A

K

D

T

R

L

L

L

T

E

D

N

A

G

G

A

A

D

E

M

T

I

V

L

I

A

S

S

R

H

M

Q

Q

D

D

I

L

A

P

A

A

R

V

L

I

A

A

binding magnesium ion: D8 (= D26), D10 (= D28), D166 (= D184)

3s6jE The crystal structure of a hydrolase from pseudomonas syringae
31% identity, 78% coverage: 24:216/246 of query aligns to 6:200/220 of 3s6jE

query
sites
3s6jE

I

I

F

F

D
|
D

F

L

D
|
D

G

G

V

T

I

L

A

T

D

D

S
|
S

E

V

V

Y

I

Q

S

N

L

V

A

A

T

A

L

W

Q

K

A

E

S

A

L

L

K

D

A

A

F

E

G

N

M

I

D

P

L

L

T

A

I

M

E

W

E

R

I

I

R

H

Q

R

K

K

F
x
I

L

G

-

M

-

S

-

G

G

G

K

L

S

M

L

L

K

K

T

S

I

L

S

S

T

R

Y

E

V

T

D

G

Q

M

H

S

S

I

S

T

S

D

Q

E

A

Q

A

A

A

E

D

R

F

L

G

S

N

E

A

K

W

-

Q

H

A

A

E

Q

L

A

Y

Y

S

E

R

R

F

L

R

Q

A

H

E

Q

L

I

K

I

P

A

L

L

P

P

H

G

L

A

E

V

K

E

L

L

F

E

E

T

L

L

A

D

E

K

T

E

A

N

T

L

R

K

F

W

C

C

I

I

A

A

S
x
T

S
|
S

G

G

T

G

F

I

E

D

R

T

I

A

N

T

V

I

A

N

L

L

S

K

A

A

M

L

S

K

M

L

S

D

D

I

C

N

F

K

D

I

H

N

V

I

F

V

S

T

S

R

E

D

Q

D

V

V

S

S

R

Y

G

G

K
|
K

P

P

A

D

P

P

D

D

L

L

F

F

L

L

M

A

A

A

E

K

A

K

L

I

D

G

V

A

S

P

P

I

S

D

R

E

C

C

L

L

V

V

I

I

E
x
G

D
|
D

S

A

L

I

Y

W

G

D

I

M

R

L

A

A

K

R

A

R

A

C

G

K

M

A

R

T

G

G

V

V

G

G

F

L

L

L

G

S

G

G

A

G

H

Y

L

D

Q

I

G

G

I

E

V

L

E

E

Q

R

H

A

G

G

active site: D8 (= D26), D10 (= D28), S16 (= S34), I44 (≠ F62), T110 (≠ S126), S111 (= S127), K143 (= K159), G167 (≠ E183), D168 (= D184)
binding calcium ion: D8 (= D26), D10 (= D28), D168 (= D184)

4eenA Crystal structure of had family hydrolase dr_1622 from deinococcus radiodurans r1 (target efi-501256) with bound magnesium
32% identity, 67% coverage: 21:186/246 of query aligns to 5:171/229 of 4eenA

query
sites
4eenA

D

D

L

A

V

V

I

L

F

F

D
|
D

F

L

D
|
D

G

G

V

V

I

L

A
x
V

D

E

S
|
S

E

E

V

G

I

I

S

I

L

A

A

Q

T

V

L

W

Q

Q

A

S

S

V

L

L

K

A

A

E

F

R

G

G

M

L

D

H

L

L

T

D

I

L

E

T

E

E

I

I

R

A

Q
x
M

K
x
Y

F

F

L
x
T

G

G

K

Q

S

R

L

F

K

D

T

G

I

V

S

L

T

A

Y

Y

V

L

D

A

Q

Q

H

Q

S

H

S

D

S

F

Q

V

A

P

D

D

F

F

G

L

N

D

A

V

W

-

Q

-

A

-

E

-

L

L

Y

E

S

T

R

R

F

F

R

N

A

A

E

A

L

M

K

T

P

G

L

V

P

T

H

A

L

I

E

E

-

G

-

A

K

E

L

T

L

L

F

R

E

A

L

L

A

R

E

A

T

A

A

G

T

V

R

P

F

F

C

A

I

I

A

G

S
|
S

S
x
N

G

S

T

E

F

R

E

G

R

R

I

L

N

H

V

L

A

K

L

L

S

R

A

V

M

A

S

G

M

L

S

T

D

E

-

L

C

A

F

G

D

E

H

H

V

I

F

Y

S

D

S

P

E

S

Q

W

V

V

S

G

-

G

R

R

G

G

K
|
K

P

P

A

H

P

P

D

D

L

L

F

Y

L

T

M

F

A

A

E

Q

A

Q

L

L

D

G

V

I

S

L

P

P

S

E

R

R

C

C

L

V

V

V

I

I

E
|
E

D
|
D

S

S

L

V

active site: D10 (= D26), D12 (= D28), V16 (≠ A32), S18 (= S34), M44 (≠ Q60), Y45 (≠ K61), T47 (≠ L63), S109 (= S126), N110 (≠ S127), K144 (= K159), E168 (= E183), D169 (= D184)
binding magnesium ion: D10 (= D26), D12 (= D28), D169 (= D184)

Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 75% coverage: 14:198/246 of query aligns to 68:256/1055 of Q8VZ10

query
sites
Q8VZ10

T

T

D

D

L

D

F

W

G

G

D

K

V

V

D

S

L

A

V

V

I

L

F

F

D
|
D

F

M

D

D

G

G

V

V

I

L

A

C

D

N

S

S

E

E

V

D

I

L

S

S

L

R

A

R

T

A

L

A

Q

V

A

D

S

V

L

F

K

T

A

E

F

M

G

G

M

V

D

E

L

V

T

T

I

V

E

D

I

F

-

V

-

P

-

F

-

M

-

G

-

T

-

G

R

E

Q

A

K

K

F

F

L

L

G

G

-

G

-

V

K

A

S

S

L

V

K

K

T

E

I

V

S

K

-

G

-

F

-

D

-

P

-

D

-

A

-

K

-

E

-

R

-

F

-

E

T

I

Y

Y

V

L

D

D

Q

K

H

Y

S

A

S

K

S

P

Q

E

A

S

A

G

A

I

D

G

F

F

G

-

N

-

A

-

W

-

Q

-

A

-

E

-

L

-

Y

-

S

-

R

-

F

-

R

-

A

-

E

-

L

-

K

-

P

-

L

-

P

P

H

G

L

A

E

L

K

E

L

L

L

V

F

T

E

E

L

C

A

K

E

N

T

K

A

G

T

L

R

K

F

V

C

A

I

V

A

A

S

S

G

A

T

D

F

R

E

I

R

K

I

V

N

D

V

A

A

N

L

L

S

K

A

A

M

A

S

G

M

L

S

S

-

L

D

T

C

M

F

F

D

D

H

A

V

I

F

V

S

S

S

A

E

D

Q

A

V

F

S

E

R

N

G

L

K

K

P

P

A

A

P

P

D

D

L

I

F

F

L

L

M

A

A

A

E

K

A

I

L

L

D

G

V

V

S

P

P

T

S

S

R

E

C

C

L

V

V

V

I

I

E

E

D

D

S

A

L

L

Y

A

G

G

I

V

R

Q

A

A

K

Q

A

A

G

N

M

M

R

R

D80 (= D26) 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.

4uasA Crystal structure of cbby from rhodobacter sphaeroides in complex with phosphate (see paper)
27% identity, 74% coverage: 20:200/246 of query aligns to 2:192/225 of 4uasA

query
sites
4uasA

V

I

D

E

L

A

V

I

I

L

F

F

D
|
D

F
x
V

D
|
D

G

G

V

T

I

L

A

A

D

E

S
x
T

E

E

V

E

I

L

S

H

L

R

A

R

T

A

L

F

Q

N

A

E

S

T

L

F

K

A

A

A

F

L

G

G

M

V

D

D

L

W

T

F

I

W

-

D

-

R

E

E

I

Y

R

R

Q

E

K

L

F

L

L
x
T

G

T

K

T

S

G

L

G

K

K

T

E

-

R

I

I

S

A

T

R

Y

F

V

L

D

R

Q

H

H

Q

S

K

S

G

S

D

Q

P

A

A

A

P

A

L

D

P

F

I

G

A

N

D

A

I

W

H

Q

R

A

A

E

K

L

-

Y

T

S

E

R

R

F

F

R

V

A

A

-

L

-

M

-

A

-

E

-

G

E

E

L

I

K

A

P

L

L

R

P

P

H

G

L

I

E

A

K

D

L

L

L

I

F

A

E

E

L

A

A

K

E

R

T

A

A

G

T

I

R

R

F

L

C

A

I

V

A

A

S
x
T

G

T

T

S

F

L

E

P

R

N

I

V

N

E

V

A

A

L

L

C

S

R

A

A

M

C

-

F

-

G

-

H

S

P

M

A

S

R

D

E

C

I

F

F

D

D

H

V

V

I

F

A

S

A

S

G

E

D

Q

M

V

V

S

A

R

E

G

K

K
|
K

P

P

A

S

P

P

D

D

L

I

F

Y

L

R

M

L

A

A

A

L

E

R

A

E

L

L

D

D

V

V

S

P

P

P

S

E

R

R

C

A

L

V

V

A

I

L

E
|
E

D
|
D

S

S

L

L

Y

N

G

G

I

L

R

R

A

A

K

K

A

G

A

A

G

G

M

L

R

R

G

C

V

I

active site: D8 (= D26), V9 (≠ F27), D10 (= D28), T16 (≠ S34), T47 (≠ L63), T115 (≠ S126), T116 (≠ S127), K151 (= K159), E175 (= E183), D176 (= D184)
binding magnesium ion: D8 (= D26), D10 (= D28), D176 (= D184)
binding phosphate ion: D8 (= D26), V9 (≠ F27), D10 (= D28), T115 (≠ S126), T116 (≠ S127), K151 (= K159)

P95649 Protein CbbY; RuCbby; EC 3.1.3.- from Cereibacter sphaeroides (Rhodobacter sphaeroides) (see paper)
27% identity, 74% coverage: 20:200/246 of query aligns to 2:192/230 of P95649

query
sites
P95649

V

I

D

E

L

A

V

I

I

L

F

F

D

D

F

V

D
|
D

G

G

V

T

I

L

A

A

D

E

S

T

E
|
E

V

E

I

L

S
x
H

L

R

A

R

T

A

L

F

Q

N

A

E

S

T

L

F

K

A

A

A

F

L

G

G

M

V

D

D

L

W

T

F

I

W

-

D

-

R

E

E

I
x
Y

R

R

Q

E

K

L

F

L

L

T

G

T

K

T

S

G

L

G

K

K

T

E

-
x
R

I

I

S

A

T

R

Y

F

V

L

D

R

Q

H

H

Q

S

K

S

G

S

D

Q

P

A

A

A

P

A

L

D

P

F

I

G

A

N

D

A

I

W

H

Q

R

A

A

E
x
K

L

-

Y

T

S

E

R

R

F

F

R

V

A

A

-

L

-

M

-

A

-

E

-

G

E

E

L

I

K

A

P

L

L

R

P

P

H

G

L

I

E

A

K

D

L

L

L

I

F

A

E

E

L

A

A

K

E

R

T

A

A

G

T

I

R

R

F

L

C

A

I

V

A

A

S

T

G

T

T

S

F

L

E

P

R

N

I

V

N

E

V

A

A

L

L

C

S

R

A

A

M

C

-

F

-

G

-

H

S

P

M

A

S

R

D

E

C

I

F

F

D

D

H

V

V

I

F

A

S

A

S

G

E

D

Q

M

V

V

S

A

R

E

G

K

K

K

P

P

A

S

P

P

D

D

L

I

F

Y

L

R

M

L

A

A

A

L

E

R

A

E

L

L

D

D

V

V

S

P

P

P

S

E

R

R

C

A

L

V

V

A

I

L

E

E

D

D

S

S

L

L

Y

N

G

G

I

L

R

R

A

A

K

K

A

G

A

A

G

G

M

L

R

R

G

C

V

I

D10 (= D28) mutation to N: Loss of catalytic activity.
E17 (= E35) 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 (≠ S38) 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 (≠ I58) 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 (vs. gap) mutation to A: 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
K78 (≠ E93) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.

4uauA Crystal structure of cbby (mutant d10n) from rhodobacter sphaeroides in complex with xylulose-(1,5)bisphosphate, crystal form ii (see paper)
26% identity, 74% coverage: 20:200/246 of query aligns to 2:192/226 of 4uauA

query
sites
4uauA

V

I

D

E

L

A

V

I

I

L

F

F

D
|
D

F
x
V

D
x
N

G

G

V

T

I

L

A

A

D

E

S
x
T

E
|
E

V

E

I

L

S
x
H

L

R

A

R

T

A

L

F

Q

N

A

E

S

T

L

F

K

A

A

A

F

L

G

G

M

V

D

D

L

W

T

F

I

W

-

D

-

R

E

E

I

Y

R

R

Q

E

K

L

F

L

L
x
T

G

T

K
x
T

S
x
G

L
x
G

K

K

T

E

-
x
R

I

I

S

A

T

R

Y

F

V

L

D

R

Q

H

H

Q

S

K

S

G

S

D

Q

P

A

A

A

P

A

L

D

P

F

I

G

A

N

D

A

I

W
x
H

Q

R

A

A

E
x
K

L

-

Y

T

S

E

R

R

F

F

R

V

A

A

-

L

-

M

-

A

-

E

-

G

E

E

L

I

K

A

P

L

L

R

P

P

H

G

L

I

E

A

K

D

L

L

L

I

F

A

E

E

L

A

A

K

E

R

T

A

A

G

T

I

R

R

F

L

C

A

I

V

A

A

S
x
T

G
x
T

T
x
S

F

L

E

P

R

N

I

V

N

E

V

A

A

L

L

C

S

R

A

A

M

C

-

F

-

G

-

H

S

P

M

A

S

R

D

E

C

I

F

F

D

D

H

V

V

I

F

A

S

A

S

G

E

D

Q

M

V

V

S

A

R

E

G

K

K
|
K

P

P

A

S

P

P

D

D

L

I

F

Y

L

R

M

L

A

A

A

L

E

R

A

E

L

L

D

D

V

V

S

P

P

P

S

E

R

R

C

A

L

V

V

A

I

L

E
|
E

D
|
D

S

S

L

L

Y

N

G

G

I

L

R

R

A

A

K

K

A

G

A

A

G

G

M

L

R

R

G

C

V

I

active site: D8 (= D26), V9 (≠ F27), N10 (≠ D28), T16 (≠ S34), T47 (≠ L63), T115 (≠ S126), T116 (≠ S127), K151 (= K159), E175 (= E183), D176 (= D184)
binding magnesium ion: D8 (= D26), N10 (≠ D28), D176 (= D184)
binding xylulose-1,5-bisphosphate: D8 (= D26), V9 (≠ F27), N10 (≠ D28), E17 (= E35), H20 (≠ S38), T49 (≠ K65), G50 (≠ S66), G51 (≠ L67), R54 (vs. gap), H75 (≠ W90), K78 (≠ E93), T115 (≠ S126), T116 (≠ S127), T117 (≠ G128), S118 (≠ T129)

P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/221 of P71447

query
sites
P71447

V

V

I

L

F

F

D
|
D

F

L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-

V

-

S

-
x
R

-

E

K

D

S
|
S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q
x
K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S

S

-

A

-

S

-

K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

K

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K

K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E

E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

D8 (= D26) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
D10 (= D28) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
T16 (≠ S34) 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 (≠ S38) 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 (≠ L63) mutation to A: 20'000-fold decrease in kcat/KM.
G46 (= G64) 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 (= S66) mutation to A: Wild-type activity.
K76 (≠ Q91) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
D170 (= D184) mutation to A: Impaired, but active with an increase in the affinity for G1P.

5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/224 of 5olwA

query
sites
5olwA

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S

H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G

G

-

V

-

S

-

R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P
|
P

-

A

-

D

-
x
V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-

S

-

K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S
x
E

A

R

M

M

S
x
N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S
|
S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding calcium ion: D8 (= D26), D10 (= D28), P89 (= P104), V92 (vs. gap), E124 (≠ S138), N127 (≠ S141), E169 (= E183), D170 (= D184), S171 (= S185)

6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/219 of 6qzgA

query
sites
6qzgA

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S

T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L

K

G
|
G

-

V

-

S

-

R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E

E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D26), L9 (≠ F27), D10 (= D28), H20 (≠ S38), G46 (= G64), S114 (= S126), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap), K145 (= K159)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/219 of 1z4nA

query
sites
1z4nA

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L
x
W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G

G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S
x
N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding 1-O-phosphono-alpha-D-galactopyranose: H20 (≠ S38), W24 (≠ L42), V47 (vs. gap), R49 (vs. gap), S116 (vs. gap), K117 (vs. gap), N118 (≠ S127)
binding magnesium ion: D8 (= D26), D10 (= D28), E169 (= E183), D170 (= D184)

2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/221 of 2wf9A

query
sites
2wf9A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S
x
N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding beryllium trifluoride ion: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), A115 (vs. gap), K145 (= K159)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D28), H20 (≠ S38), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S116 (vs. gap), K117 (vs. gap), N118 (≠ S127)
binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D28), H20 (≠ S38), G46 (= G64), V47 (vs. gap), R49 (vs. gap), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap), N118 (≠ S127)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/221 of 1o03A

query
sites
1o03A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D26), L9 (≠ F27), D10 (= D28), H20 (≠ S38), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S114 (= S126), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap), K145 (= K159)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/221 of 1lvhA

query
sites
1lvhA

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S

H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G

G

-

V

-

S

-

R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-

S

-

K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 6h91A

query
sites
6h91A

V

V

I

L

F

F

D
|
D

F

L

D
|
D

G

G

V

V

I

I

A

T

D

D

S

T

E

A

V

E

I

Y

S

H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L

K

G

G

-

V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S

S

-

A

-

S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K

K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E

E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)
binding acetylphosphate: R49 (vs. gap), K117 (vs. gap)

4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 4c4rA

query
sites
4c4rA

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L
x
W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F
x
L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S
|
S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)
binding trifluoromagnesate: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), A115 (vs. gap), K145 (= K159)
binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D28), H20 (≠ S38), W24 (≠ L42), L44 (≠ F62), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S52 (= S66), S116 (vs. gap), K117 (vs. gap)

3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 3zi4A

query
sites
3zi4A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D28), H20 (≠ S38), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S116 (vs. gap), K117 (vs. gap)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)
binding Scandium Tetrafluoride: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), A115 (vs. gap), K145 (= K159)

2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 2wf8A

query
sites
2wf8A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S
x
H

L

F

A

R

T

A

L
x
W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F
x
L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S
|
S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding beryllium trifluoride ion: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), A115 (vs. gap), K145 (= K159)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D28), H20 (≠ S38), G46 (= G64), V47 (vs. gap), R49 (vs. gap), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap)
binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D28), H20 (≠ S38), W24 (≠ L42), L44 (≠ F62), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S52 (= S66), A115 (vs. gap), S116 (vs. gap), K117 (vs. gap)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 2wf7A

query
sites
2wf7A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S

H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S
x
N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding tetrafluoroaluminate ion: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), K145 (= K159)
binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D28), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S116 (vs. gap), K117 (vs. gap), N118 (≠ S127)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
28% identity, 73% coverage: 23:201/246 of query aligns to 5:187/218 of 2wf6A

query
sites
2wf6A

V

V

I

L

F

F

D
|
D

F
x
L

D
|
D

G

G

V

V

I

I

A

T

D

D

S
x
T

E

A

V

E

I

Y

S

H

L

F

A

R

T

A

L

W

Q

K

A

A

S

L

L

A

K

E

A

E

F

I

G

G

M

I

D

N

L

G

T

V

I

D

E

R

E

Q

I

F

R

N

Q

E

K

Q

F

L

L
x
K

G
|
G

-
x
V

-

S

-
x
R

-

E

K

D

S

S

L

L

K

Q

T

K

I

I

S

L

T

D

Y

L

V

A

D

D

Q

K

H

K

S

V

S

S

S

A

Q

E

A

E

A

F

A

K

D

E

F

L

G

A

N

K

A

R

W

-

Q

K

A

N

E

D

L

N

Y

Y

S

V

R

K

F

M

R

I

A

Q

E

D

L

V

K

S

P

P

-

A

-

D

-

V

L

Y

P

P

H

G

L

I

E

L

K

Q

L

L

F

K

E

D

L

L

A

R

E

S

T

N

A

K

T

I

R

K

F

I

C

A

I

L

A

A

S
|
S

-
x
A

-
x
S

-
x
K

S

N

G

G

T

P

F

F

E

-

R

-

I

-

N

-

V

-

A

L

L

L

S

E

A

R

M

M

S

N

M

L

S

T

D

G

C

Y

F

F

D

D

H

A

V

I

F

A

S

D

S

P

E

A

Q

E

V

V

S

A

R

A

G

S

K
|
K

P

P

A

A

P

P

D

D

L

I

F

F

L

I

M

A

A

A

E

H

A

A

L

V

D

G

V

V

S

A

P

P

S

S

R

E

C

S

L

I

V

G

I

L

E
|
E

D
|
D

S

S

L

Q

Y

A

G

G

I

I

R

Q

A

A

A

I

K

K

A

D

A

S

G

G

M

A

R

L

G

P

V

I

G

G

active site: D8 (= D26), L9 (≠ F27), D10 (= D28), T16 (≠ S34), K45 (≠ L63), S114 (= S126), A115 (vs. gap), K145 (= K159), E169 (= E183), D170 (= D184)
binding tetrafluoroaluminate ion: D8 (= D26), L9 (≠ F27), D10 (= D28), S114 (= S126), K145 (= K159)
binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D28), G46 (= G64), V47 (vs. gap), R49 (vs. gap), S116 (vs. gap), K117 (vs. gap)
binding magnesium ion: D8 (= D26), D10 (= D28), D170 (= D184)

Query Sequence

>3607123 FitnessBrowser__Dino:3607123
MNTPRKLRLPQTCTDLFGDVDLVIFDFDGVIADSEVISLATLQASLKAFGMDLTIEEIRQ
KFLGKSLKTISTYVDQHSSSQAAADFGNAWQAELYSRFRAELKPLPHLEKLLFELAETAT
RFCIASSGTFERINVALSAMSMSDCFDHVFSSEQVSRGKPAPDLFLMAAEALDVSPSRCL
VIEDSLYGIRAAKAAGMRGVGFLGGAHLQGIVEQHGKTLLENGADMILASHQDIAARLAP
KRTQQN

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