SitesBLAST

M1 (= M1) modified: Initiator methionine, Removed
C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
H30 (= H25) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D29) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y73) mutation to A: 5-fold decrease in glutamine affinity.
A105 (vs. gap) mutation to H: Little effect on the kinetic properties.
E349 (= E328) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
35% identity, 59% coverage: 3:337/570 of query aligns to 2:341/497 of 1ct9A

query
sites
1ct9A

A

S

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I

F

F

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G

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D

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I

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K

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D

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x
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Y

active site: L50 (= L46), N74 (= N67), G75 (= G68), T305 (≠ S304), R308 (vs. gap), E332 (= E328)
binding adenosine monophosphate: L232 (= L226), L233 (= L227), S234 (= S228), S239 (= S233), A255 (≠ S251), V256 (≠ I252), D263 (≠ E261), M316 (≠ L312), S330 (= S326), G331 (= G327), E332 (= E328)
binding glutamine: R49 (= R45), L50 (= L46), I52 (= I48), V53 (≠ L49), N74 (= N67), G75 (= G68), E76 (= E69), D98 (≠ E80)

Sites not aligning to the query:

active site: 1, 366
binding glutamine: 1

P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 77% coverage: 1:437/570 of query aligns to 1:478/557 of P78753

query
sites
P78753

M

M

C

C

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x
S

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A

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D

D

S391 (≠ K359) modified: Phosphoserine

Sites not aligning to the query:

489 modified: Phosphoserine

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
29% identity, 59% coverage: 2:337/570 of query aligns to 1:361/509 of 6gq3A

query
sites
6gq3A

C
|
C

A

G

I

I

F
x
W

G

A

V

L

I

F

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G

K

S

I

D

D

D

-

C

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A

A

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S

A

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G

E

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D

D

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A

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F

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F

S

E

G

N

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Y

N

E

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E

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G

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C

F

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L

F

A

G

H

F

H

H

R
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R

L
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L

Y

A

I
x
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L
x
V

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D

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P

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L

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F

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M

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K

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D

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A

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K

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P

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Y

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W

N

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S

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K

-

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-

L

L

L

C

F
x
Y

N
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N

G
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G

E
|
E

I

I

Y

Y

N

N

Y

H

E

K

-

K

-

M

-

Q

-

H

-

F

-

E

-

F

D

E

F

Y

H

Q

T

T

S

K

E
x
V

A
x
D

A

G

A

E

I

I

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I

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M

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D

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G

M

V

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F

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A

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L

D

D

-

T

-

A

K

N

E

K

K

K

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L

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R

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D

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K

E

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L

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D

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A

C

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M

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D

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x
T

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x
R

A

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M

F

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Y

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-

F

S

S

G

G

E

E

G

G

G

S

D

D

E

E

I

L

F

T

L

Q

G

G

Y

Y

active site: W4 (≠ F5), L49 (= L46), N74 (= N67), G75 (= G68), T324 (≠ S304), R327 (vs. gap)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R45), V51 (≠ I48), V52 (≠ L49), Y73 (≠ F66), N74 (= N67), G75 (= G68), E76 (= E69), V95 (≠ E80), D96 (≠ A81)

P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
27% identity, 59% coverage: 1:337/570 of query aligns to 1:374/561 of P08243

query
sites
P08243

M

M

C
|
C

A

G

I

I

F

W

G
x
A

V

L

I

F

G

G

K

S

I

D

D

D

-

C

-

L

R

S

E

V

K

Q

A

C

L

L

N

S

A

A

F

M

S

K

L

I

L

-

S

A

H

H

R

R

G

G

E

P

D

D

E

A

-

F

-

R

-

F

S

E

G

N

V

V

Y

N

E

G

R

Y

E

T

G

N

V

C

F

C

L

F

A

G

H

F

H

H

R

R

L

L

Y

A

I

V

L

V

N

D

-

P

-

L

-

F

-

G

-

M

-

Q

-

P

-

I

K

R

D

V

A

K

K

K

Q

Y

P

P

F

Y

V

L

Q

W

N

-

S

-

K

-

V

-

L

L

L

C

F

Y

N

N

G

G

E

E

I

I

Y

Y

N

N

Y

H

E

K

-

K

-

M

-

Q

-

H

-

F

-

E

-

F

D

E

F

Y

H

Q

T

T

S

K

E

V

A

D

A

G

A

E

I

I

L

I

-

L

-

H

-

L

-

Y

-

D

-

K

-

G

E

G

V

I

A

E

P

Q

D

T

F

I

S

C

K

M

L

L

D

D

G

G

M

V

F

F

A

A

L

F

A

V

L

L

D

D

-

T

-

A

K

N

E

K

K

K

L

V

Y

F

L

L

A

G

R

R

D

D

L

T

F

Y

G

G

K

V

K

R

P

P

L

L

Y

F

Y

K

A

A

F

M

W

T

Q

E

D

D

S

G

F

F

I

L

-

A

F

V

A

C

S

S

E

E

I

A

K

K

A

G

I

L

L

V

A

T

Y

L

T

K

N

H

E

-

Q

-

K

-

I

-

N

-

A

-

R

-

A

-

L

-

S

-

Y

-

L

-

S

S

F

A

G

T

A

P

V

F

V

L

G

K

R

V

E

E

T

P

F

F

Y

L

E

P

G

G

I

H

Y

Y

K

E

L

V

-

L

-

D

-

L

-

K

D

P

G

N

G

G

E

K

I

V

L

A

E

S

L

V

D

E

I

M

K

V

R

K

L

-

Y

Y

Y

H

A

H

C

C

K

R

R

D

F
x
V

T

P

T

L

L

H

-

A

-

L

-

Y

-

D

-

N

-

V

-

E

-

K

-

L

-

F

-

P

-

G

-

F

-

E

L

I

Q

E

K

T

R

V

S

K

G

N

D

N

L

L

K

R

R

I

L

L

L

F

V

N

A

N

A

A

V

V

K

K

R

R

L

L

Q

M

G

T

D

D

F

R

P

R

A

I

V

G

A

C

L

L

S

S

G

G

V

L

D

D

S

S

F

L

V

V

S

A

A

A

I

T

-

L

-

K

-

Q

-

L

-

K

A

E

K

A

R

Q

L

V

Q

Q

G

Y

S

P

L

L

A

Q

T

T

Y

F

S

A

I

I

G

G

Y

M

E

E

E

D

G

S

R

-

Y

-

S

P

E

D

L

L

P

L

Y

A

A

A

Q

R

E

K

V

V

A

A

Q

D

Y

H

I

I

G

G

S

S

D

E

H

H

H

Y

E

E

I

V

I

L

F

F

T

N

K

S

D

E

F

G

F

I

A

Q

T

A

L

L

E

D

R

E

A

V

S

-

I

I

F

F

F

S

D

L

E

E

P

T

I

Y

G

D

D

I

S

T

-

T

-

V

-

R

A

A

S

S

L

V

P

G

L

M

F

Y

Y

L

L

I

M

S

E

K

R

Y

I

I

K

R

K

K

D

N

G

T

A

D

K

S

V

V

L

I

-
x
F

S

S

G

G

E

E

G

G

G

S

D

D

E

E

I

L

F

T

L

Q

G

G

Y

Y

C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
A6 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
V210 (≠ F194) to E: in dbSNP:rs1049674
F362 (vs. gap) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973

Sites not aligning to the query:

550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974

1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 35% coverage: 91:290/570 of query aligns to 111:306/500 of 1jgtB

query
sites
1jgtB

F

F

S

R

K

L

L

V

D

N

G

G

M

R

F

F

A

A

L

T

A

V

L

V

L

R

D

T

K

G

E

D

K

R

L

V

Y

L

L

L

A

A

R

T

D

D

L

H

F

A

G

G

K

S

K

V

P

P

L

L

Y

Y

Y

T

A

C

F

V

W

A

Q

P

D

G

S

E

F

V

I

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

I

L

L

A

A

A

Y

H

T

R

N

D

E

P

Q

K

K

G

-

F

-

P

-

L

I

A

N

D

A

A

R

R

A

-

L

-

S

-

Y

-

L

-

S

-

F

-

G

-

A

-

V

-

G

-

R

R

E

V

T

A

F

G

Y

L

E

T

G

G

I

V

Y

Y

K

Q

L

V

D

P

G

A

G

G

E

A

I

V

L

M

E

D

L

I

D

D

I

L

K

G

R

S

L

G

Y

T

Y

A

A

V

C

T

K

H

R

R

-

T

F

W

T

T

T

P

L

G

L

L

Q

S

K

R

R

R

-

I

-

L

-

P

S

E

G

G

D

E

L

A

K

V

R

A

L

A

L

V

V

R

A

A

V

L

K

E

K

K

R

A

L

V

-

A

-

Q

-

R

-

V

-

T

Q

P

G

G

D

D

F

T

P

P

A

L

V

V

A

-

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V
x
I

D
|
D

S
|
S

S

S

F

G

V

V

S

A

A

A

I

C

A

A

K

H

R

R

L

A

Q

A

G

G

S

E

L

L

A

D

T

T

Y

V

S
|
S

I
x
M

G

G

Y

T

E

D

E

T

G

-

R

-

Y

S

S

N

E

E

L

F

P

R

Y

E

A

A

Q

R

E

A

V

V

A

V

Q

D

Y

H

I

L

G

R

S

T

D

R

H

H

H

R

E

E

I

I

I

T

F

I

T

P

K

T

D

T

D

E

F

L

A

A

T

Q

L

L

binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L226), L245 (= L227), S246 (= S228), G248 (= G230), I249 (≠ V231), D250 (= D232), S251 (= S233), S269 (= S251), M270 (≠ I252)
binding magnesium ion: D250 (= D232)

Sites not aligning to the query:

active site: 73, 74, 319, 345, 379, 440
binding diphosphomethylphosphonic acid adenosyl ester: 327, 344, 345, 348, 420, 440
binding n2-(carboxyethyl)-l-arginine: 323, 345, 346, 348, 349, 354, 370, 379
binding magnesium ion: 348

1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 35% coverage: 91:290/570 of query aligns to 108:297/485 of 1mb9A

query
sites
1mb9A

F

F

S

R

K

L

L

V

D

N

G

G

M

R

F

F

A

A

L

T

A

V

L

V

L

R

D

T

K

G

E

D

K

R

L

V

Y

L

L

L

A

A

R

T

D

D

L

H

F

A

G

G

K

S

K

V

P

P

L

L

Y

Y

Y

T

A

C

F

V

W

A

Q

P

D

G

S

E

F

V

I

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

I

L

L

A

A

A

Y

F

T

-

N

-

E

-

Q

P

K

L

I

A

N

D

A

A

R

R

A

-

L

-

S

-

Y

-

L

-

S

-

F

-

G

-

A

-

V

-

G

-

R

R

E

V

T

A

F

G

Y

L

E

T

G

G

I

V

Y

Y

K

Q

L

V

D

P

G

A

G

G

E

A

I

V

L

M

E

D

L

I

D

D

I

L

K

G

R

S

L

G

Y

T

Y

A

A

V

C

T

K

H

R

R

F

T

T

W

T

T

L

-

Q

-

K

-

R

-

S

P

G

G

D

L

L

S

K

R

R

R

L

I

L

L

-

P

-

E

-

G

-

E

-

A

V

V

A

A

V

V

K

R

K

A

R

A

L

L

Q

E

-

K

-

A

-

V

-

A

-

Q

-

R

-

V

-

T

-

P

G

G

D

D

F

T

P

P

A

L

V

V

A

-

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

F

G

V

V

S

A

A

A

I

C

A

A

K

H

R

R

L

A

Q

A

G

G

S

E

L

L

A

D

T

T

Y

V

S
|
S

I
x
M

G

G

Y

T

E

D

E

T

G

-

R

-

Y

S

S

N

E

E

L

F

P

R

Y

E

A

A

Q

R

E

A

V

V

A

V

Q

D

Y

H

I

L

G

R

S

T

D

R

H

H

H

R

E

E

I

I

I

T

F

I

T

P

K

T

D

T

D

E

F

L

A

A

T

Q

L

L

binding adenosine monophosphate: V235 (≠ L226), L236 (= L227), S242 (= S233), S260 (= S251), M261 (≠ I252)
binding adenosine-5'-triphosphate: V235 (≠ L226), L236 (= L227), S237 (= S228), G239 (= G230), D241 (= D232), S242 (= S233), S260 (= S251), M261 (≠ I252)
binding magnesium ion: D241 (= D232)
binding pyrophosphate 2-: S237 (= S228), G239 (= G230), D241 (= D232), S242 (= S233)

Sites not aligning to the query:

active site: 70, 71, 310, 336, 370, 431
binding adenosine monophosphate: 314, 318, 335, 336
binding adenosine-5'-triphosphate: 318, 335, 339, 411, 431
binding magnesium ion: 339
binding pyrophosphate 2-: 339, 411, 431

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 35% coverage: 91:290/570 of query aligns to 107:298/496 of 1mbzA

query
sites
1mbzA

F

F

S

R

K

L

L

V

D

N

G

G

M

R

F

F

A

A

L

T

A

V

L

V

L

R

D

T

K

G

E

D

K

R

L

V

Y

L

L

L

A

A

R

T

D

D

L

H

F

A

G

G

K

S

K

V

P

P

L

L

Y

Y

Y

T

A

C

F

V

W

A

Q

P

D

G

S

E

F

V

I

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

I

L

L

A

A

A

Y

H

T

-

N

G

E

F

Q

P

K

L

I

A

N

D

A

A

R

R

A

-

L

-

S

-

Y

-

L

-

S

-

F

-

G

-

A

-

V

-

G

-

R

R

E

V

T

A

F

G

Y

L

E

T

G

G

I

V

Y

Y

K

Q

L

V

D

P

G

A

G

G

E

A

I

V

L

M

E

D

L

I

D

D

I

L

K

G

R

S

L

G

Y

T

Y

A

A

V

C

T

K

H

R

R

-

T

F

W

T

T

T

P

L

G

L

L

Q

S

K

R

R

R

-

I

-

L

-

P

S

E

G

G

D

E

L

A

K

V

R

A

L

A

L

V

V

R

A

A

V

L

K

E

K

K

R

A

L

V

-

A

-

Q

-

R

-

V

-

T

Q

P

G

G

D

D

F

T

P

P

A

L

V

V

A

-

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

F

G

V

V

S

A

A

A

I

C

A

A

K

H

R

R

L

A

Q

A

G

G

S

E

L

L

A

D

T

T

Y

V

S
|
S

I
x
M

G

G

Y

T

E

D

E

T

G

-

R

-

Y

S

S

N

E

E

L

F

P

R

Y

E

A

A

Q

R

E

A

V

V

A

V

Q

D

Y

H

I

L

G

R

S

T

D

R

H

H

H

R

E

E

I

I

I

T

F

I

T

P

K

T

D

T

D

E

F

L

A

A

T

Q

L

L

binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L226), L237 (= L227), S238 (= S228), S243 (= S233), S261 (= S251), M262 (≠ I252)
binding magnesium ion: D242 (= D232)
binding pyrophosphate 2-: S238 (= S228), G240 (= G230), D242 (= D232), S243 (= S233)

Sites not aligning to the query:

active site: 69, 70, 311, 337, 371, 432
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 315, 319, 336, 337, 338, 340, 341, 362, 371, 432, 434, 435
binding magnesium ion: 340
binding pyrophosphate 2-: 340, 412, 432, 433

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 35% coverage: 91:290/570 of query aligns to 103:293/491 of 1mc1A

query
sites
1mc1A

F

F

S

R

K

L

L

V

D

N

G

G

M

R

F

F

A

A

L

T

A

V

L

V

L

R

D

T

K

G

E

D

K

R

L

V

Y

L

L

L

A

A

R

T

D

D

L

H

F

A

G

G

K

S

K

V

P

P

L

L

Y

Y

Y

-

A

-

F

-

W

-

Q

-

D

-

S

T

F

C

I

V

F

A

A

P

S

G

E

E

I

V

K

R

A

A

I

-

L

-

A

-

Y

-

T

-

N

-

E

-

Q

-

K

S

I

T

N

E

A

A

R

K

A

A

L

L

S

A

Y

G

L

F

S

P

F

L

G

-

A

A

V

D

V

A

G

R

R

R

E

V

T

A

F

G

Y

L

E

T

G

G

I

V

Y

Y

K

Q

L

V

D

P

G

A

G

G

E

A

I

V

L

M

E

D

L

I

D

D

I

L

K

G

R

S

L

G

Y

T

Y

A

A

V

C

T

K

H

R

R

F

T

T

W

T

T

L

-

Q

-

K

-

R

-

S

P

G

G

D

L

L

S

K

R

R

R

L

I

L

L

-

P

-

E

-

G

-

E

-

A

V

V

A

A

V

V

K

R

K

A

R

A

L

L

Q

E

-

K

-

A

-

V

-

A

-

Q

-

R

-

V

-

T

-

P

G

G

D

D

F

T

P

P

A

L

V

V

A

-

L
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

F

G

V

V

S

A

A

A

I

C

A

A

K

H

R

R

L

A

Q

A

G

G

S

E

L

L

A

D

T

T

Y

V

S
|
S

I
x
M

G

G

Y

T

E

D

E

T

G

-

R

-

Y

S

S

N

E

E

L

F

P

R

Y

E

A

A

Q

R

E

A

V

V

A

V

Q

D

Y

H

I

L

G

R

S

T

D

R

H

H

H

R

E

E

I

I

I

T

F

I

T

P

K

T

D

T

D

E

F

L

A

A

T

Q

L

L

binding adenosine monophosphate: V231 (≠ L226), S233 (= S228), S238 (= S233), S256 (= S251), M257 (≠ I252)
binding magnesium ion: D237 (= D232)
binding pyrophosphate 2-: S233 (= S228), G235 (= G230), D237 (= D232), S238 (= S233)

Sites not aligning to the query:

active site: 65, 66, 306, 332, 366, 427
binding adenosine monophosphate: 331, 427, 430
binding magnesium ion: 335
binding deoxyguanidinoproclavaminic acid: 310, 332, 333, 336, 357, 366, 427
binding pyrophosphate 2-: 335, 407, 427, 428

Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
34% identity, 19% coverage: 227:336/570 of query aligns to 245:353/503 of Q9XB61

query
sites
Q9XB61

L
|
L

S
|
S

G
|
G

V
x
L

D
|
D

S
|
S

S

S

F

L

V

V

S

T

A

A

I

L

A

A

K

S

R

R

L

H

Q

F

G

K

S

K

L

L

A

N

T

T

Y

Y

S

S

I
|
I

G

G

Y

T

E

E

E

-

G

-

R

L

Y

S

S

N

E

E

L

F

P

E

Y

F

A

S

Q

Q

E

Q

V

V

A

A

Q

D

Y

A

I

L

G

G

S

T

D

H

H

H

H

Q

E

M

I

K

I

I

F

L

T

S

K

E

D

T

D

E

F

V

F

I

A

N

T

G

L

I

E

I

R

E

A

-

S

S

I

I

F

Y

D

N

E

E

P

-

I

I

G

F

D

D

S

G

A

L

S

S

L

A

P

E

L

I

-

Q

-

S

-

G

F

L

Y

F

L

N

M

V

E

Y

R

R

I

Q

K

A

K

Q

D

G

G

Q

A

V

K

S

V

C

V

M

L

L

S

T

G
|
G

E
x
Y

G
|
G

G
x
S

D
|
D

E

L

I

L

F

F

L

G

G

G

I270 (= I252) binding ATP
GYGSD 344:348 (≠ GEGGD 327:331) binding ATP
Y345 (≠ E328) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G329) binding substrate

Sites not aligning to the query:

244:251 binding ATP
371 binding substrate
374 binding substrate
380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
421 binding ATP
443 mutation K->A,M: Loss of activity.
444:446 binding ATP

1q19A Carbapenam synthetase (see paper)
34% identity, 19% coverage: 227:336/570 of query aligns to 244:352/500 of 1q19A

query
sites
1q19A

L
|
L

S
|
S

G

G

V

L

D
|
D

S
|
S

S

S

F

L

V

V

S

T

A

A

I

L

A

A

K

S

R

R

L

H

Q

F

G

K

S

K

L

L

A

N

T

T

Y

Y

S
|
S

I
|
I

G

G

Y

T

E

E

E

-

G

-

R

L

Y

S

S

N

E

E

L

F

P

E

Y

F

A

S

Q

Q

E

Q

V

V

A

A

Q

D

Y

A

I

L

G

G

S

T

D

H

H

H

H

Q

E

M

I

K

I

I

F

L

T

S

K

E

D

T

D

E

F

V

F

I

A

N

T

G

L

I

E

I

R

E

A

-

S

S

I

I

F

Y

D

N

E

E

P

-

I

I

G

F

D

D

S

G

A
x
L

S

S

L

A

P
x
E

L

I

-

Q

-

S

-

G

F

L

Y

F

L

N

M

V

E

Y

R

R

I

Q

K

A

K

Q

D

G

G

Q

A

V

K

S

V

C

V

M

L

L

S
x
T

G
|
G

E
x
Y

G
|
G

G

S

D
|
D

E
x
L

I

L

F

F

L

G

G

G

active site: L318 (≠ A305), E321 (≠ P308), Y344 (≠ E328)
binding diphosphomethylphosphonic acid adenosyl ester: L244 (= L227), S245 (= S228), D249 (= D232), S250 (= S233), S268 (= S251), I269 (= I252), T342 (≠ S326), G343 (= G327), D347 (= D331)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E328), G345 (= G329), L348 (≠ E332)

Sites not aligning to the query:

active site: 56, 379, 442
binding diphosphomethylphosphonic acid adenosyl ester: 243, 442, 443, 444, 445
binding (2s,5s)-5-carboxymethylproline: 373, 379

Query Sequence

>WP_084274777.1 NCBI__GCF_900176045.1:WP_084274777.1
MCAIFGVIGKIDREKALNAFSLLSHRGEDESGVYEREGVFLAHHRLYILNKDAKQPFVQN
SKVLLFNGEIYNYEDFHTSEAAAILEVAPDFSKLDGMFALALLDKEKLYLARDLFGKKPL
YYAFWQDSFIFASEIKAILAYTNEQKINARALSSYLSFGAVVGRETFYEGIYKLDGGEIL
ELDIKRLYYACKRFTTLLQKRSGDLKRLLVAAVKKRLQGDFPAVALLSGGVDSSFVSAIA
KRLQGSLATYSIGYEEGRYSELPYAQEVAQYIGSDHHEIIFTKDDFFATLERASIFFDEP
IGDSASLPLFYLMERIKKDGAKVVLSGEGGDEIFLGYRQYFEFFDLYKARDLKYKNWLKN
YFRSNFSPNKEWEWYKRVFSDEVIFRSSCEVFTDLQKNLFLRQNVKDNESLQVLQPYLEE
WERSGWKDGAAFFTYIDIKVRLQSLYLAKLDTTSMAYTIEARTPLLDSSVLYSAFADPQR
SKAPKYLLKKIASKYIPQSIIERKKRGFSYPALEWLQSSGSDQKLREANKRFHLFKQEQL
EFLIENAKRNRFTRHYWLVYALLDWMERKF

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