SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_046158015.1 NCBI__GCF_000971335.1:WP_046158015.1 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)

P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
68% identity, 99% coverage: 1:303/306 of query aligns to 1:306/311 of P0A786

query
sites
P0A786

M
|
M

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T

T

R
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R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K

K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
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R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
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H

P

P

T

T

Q
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Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

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L

T

H

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V

A

A

F

M

A

V

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G

D

D

L

L

K

K

Y

Y

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G

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R

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T

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V

H

H

S

S

L

L

A

T

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Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

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R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

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Y

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E

E

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M

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A

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E

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D

V

I

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L

Y

Y

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M

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T

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R

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E

E

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D

D

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A

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Y

F

A

V

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L

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R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P

P

L
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L

P
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P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G

G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

M1 (= M1) modified: Initiator methionine, Removed
R55 (= R55) binding carbamoyl phosphate
T56 (= T56) binding carbamoyl phosphate
R106 (= R105) binding carbamoyl phosphate
H135 (= H133) binding carbamoyl phosphate
Q138 (= Q136) binding carbamoyl phosphate
L268 (= L265) binding carbamoyl phosphate
P269 (= P266) binding carbamoyl phosphate

2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2ipoA

query
sites
2ipoA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

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S

C

C

F

F

F

F

E

E

P

A

S
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S

T
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T

R
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R

T
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T

R

R

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L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
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K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

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I

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S

T

Y

Y

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V

D

D

A

A

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V

M

M

R
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R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
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H

P

P

T

T

Q
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Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
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R

T
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T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

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C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

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A

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S

L

I

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E

E

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V

I

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P

A

E

E

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D

D

V

I

L

L

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Y

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M

T
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T

R
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R

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V

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Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
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P

L
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L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
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G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), R167 (= R166), T168 (= T167), R229 (= R227), L267 (= L265)

2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2h3eA

query
sites
2h3eA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
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S

T
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T

R
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R

T
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T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
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K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
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R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
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H

P

P

T

T

Q
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Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
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R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

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A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

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V

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M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
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T

R
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R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
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P

L
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L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), R167 (= R166), R229 (= R227), L267 (= L265)

2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2fzkA

query
sites
2fzkA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
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R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R

R

T
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T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

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I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

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Y

Y

I

I

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E

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E

M

L

L

D

D

E

E

K

K

G

G

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I

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A

Y

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A

H

A

S

S

S

L

I

E

E

E

E

V

V

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M

P

A

E

E

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V

D

D

V

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L

Y

Y

M

M

T
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T

R
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R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
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P

L
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L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R
|
R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T56), H134 (= H133), Q137 (= Q136), T168 (= T167), R229 (= R227), P266 (= P264), L267 (= L265), R296 (= R294)

2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2fzgA

query
sites
2fzgA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T
|
T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R
|
R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), R167 (= R166), T168 (= T167), R229 (= R227), P266 (= P264), L267 (= L265)

2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2fzcA

query
sites
2fzcA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T
|
T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R105), R167 (= R166), T168 (= T167), P266 (= P264), L267 (= L265)

2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2airA

query
sites
2airA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R

R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S53), T53 (= T54), R54 (= R55), R105 (= R105)
binding phosphoric acid mono(formamide)ester: R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133)

1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 1za2A

query
sites
1za2A

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T
|
T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T
|
T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding phosphoric acid mono(formamide)ester: T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), R167 (= R166), T168 (= T167), L267 (= L265)

1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 1r0cA

query
sites
1r0cA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R

R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding n-carbamoyl-l-aspartate: S52 (= S53), R54 (= R55), R105 (= R105)
binding phosphate ion: R105 (= R105), H134 (= H133), Q137 (= Q136)

1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 1r0bA

query
sites
1r0bA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S
|
S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R
|
R

V

V

Q
|
Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L

L

P
|
P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding citrate anion: H134 (= H133), R167 (= R166), R229 (= R227), Q231 (= Q229), P266 (= P264), P268 (= P266)
binding phosphate ion: S80 (= S81), K84 (= K84)

5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/309 of 5vmqC

query
sites
5vmqC

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
x
A

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R

R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E
|
E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M
x
D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), A105 (≠ R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding calcium ion: E216 (= E214), D253 (≠ M251)

2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2hseA

query
sites
2hseA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

L

L

S
|
S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R
|
R

V

V

Q
|
Q

R

K

E

E

R

R

F

L

D

A

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L
|
L

P
|
P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A
|
A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R
|
R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding aspartic acid: R54 (= R55), T55 (= T56), S58 (= S59), R105 (= R105), H134 (= H133), Q137 (= Q136), R167 (= R166), R229 (= R227), Q231 (= Q229), L267 (= L265), P268 (= P266), A289 (= A287), R296 (= R294)
binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), L267 (= L265)

2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
68% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2a0fA

query
sites
2a0fA

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

E

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

E

T

T

Q

Q

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R

R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

Q

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R

R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

A

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding phosphonoacetamide: R54 (= R55), T55 (= T56), H134 (= H133), Q137 (= Q136), L267 (= L265)

2at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral ph (see paper)
67% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 2at1A

query
sites
2at1A

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L

L

L

Q

K

D

H

K

K

L

V

V

I

A

A

S

S

C

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

L

L

S

S

F

F

E

Q

T

T

A

S

V

M

Q

H

R

R

L

L

G

G

G

A

N

S

I

V

I

V

G

G

F

F

A

S

D

D

G

S

G

A

N

N

T

T

S

S

-

L

A

G

K

K

K
|
K

G

G

E

E

T

T

L

L

A

A

D

D

S

T

I

I

K

S

I

V

I

I

S

S

S

T

Y

Y

T

V

D

D

A

A

V

I

V

V

M

M

R
|
R

H

H

P

P

K

Q

E

E

G

G

A

A

A

A

R

R

L

L

A

A

S

T

E

E

F

F

S

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

N

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

F

F

S

T

I

I

R

Q

E

Q

T

T

Q

E

G

G

R

R

L

L

D

D

G

N

L

L

T

H

V

V

A

A

F

M

A

V

G

G

D

D

L

L

K

K

Y

Y

G

G

R
|
R

T

T

V

V

H

H

S

S

L

L

A

T

Q

Q

A

A

L

L

S

A

L

K

F

F

-

D

G

G

A

N

R

R

F

F

Y

Y

F

F

V

I

S

A

P

P

E

D

V

A

L

L

A

A

M

M

P

P

D

E

Y

Y

I

I

C

L

E

D

E

M

L

L

D

D

E

E

K

K

G

G

I

I

S

A

Y

W

T

S

V

L

A

H

A

S

S

S

L

I

E

E

E

E

V

V

I

M

P

A

E

E

V

V

D

D

V

I

L

L

Y

Y

M

M

T
|
T

R
|
R

V

V

Q

Q

R

K

E

E

R

R

F

L

D

D

E

P

A

S

E

E

F

Y

R

A

K

N

I

V

Q

K

G

A

Q

Q

Y

F

A

V

L

L

R

R

A

A

D

S

M

D

L

L

K

H

N

N

A

A

R

K

P

A

G

N

M

M

K

K

V

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

V

T

D

D

V

V

D

D

A

K

T

T

P

P

H

H

A

A

Y

W

Y

Y

F

F

E

Q

Q

Q

A

A

K

G

N

N

G
|
G

V

I

Y

F

A

A

R

R

Q

Q

A

A

L

L

L

L

S

A

L

L

V

V

L

L

N

N

active site: R54 (= R55), T55 (= T56), K84 (= K84), R105 (= R105), H134 (= H133), Q137 (= Q136), T228 (= T226), P266 (= P264), G292 (= G290)
binding alpha-D-glucopyranose: R167 (= R166), R229 (= R227)
binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R105), H134 (= H133), Q137 (= Q136)

1at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral p H (see paper)
67% identity, 99% coverage: 2:303/306 of query aligns to 1:305/310 of 1at1A

query
sites
1at1A

A

A

N

N

P

P

L

L

Y

Y

R

Q

K

K

H

H

I

I

I

I

S

S

I

I

P

N

D

D

F

L

S

S

R

R

E

D

E

D

L

L

E

N

L

L

V

V

V

L

D

A

T

T

A

A

A

A

R

K

L

L

K

K

Q

A

T

N

P

P

R

Q

G

P

D

E

L

L