SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_007693507.1 NCBI__GCF_000336675.1:WP_007693507.1 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)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
55% identity, 97% coverage: 5:305/310 of query aligns to 1:304/307 of 1ml4A

query
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1ml4A

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active site: R56 (= R57), T57 (= T58), K85 (= K86), R106 (= R107), H134 (= H135), Q137 (= Q138), T227 (= T228), P266 (= P267), G292 (= G293)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S55), T55 (= T56), R56 (= R57), T57 (= T58), R106 (= R107), H134 (= H135), R167 (= R168), T168 (= T169), R228 (= R229), L267 (= L268)

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
50% identity, 95% coverage: 11:306/310 of query aligns to 4:301/304 of 4eknB

query
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4eknB

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active site: T225 (= T228), P262 (= P267), G288 (= G293)
binding sulfate ion: G163 (= G167), R164 (= R168), T165 (= T169), R226 (= R229)

P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
48% identity, 96% coverage: 10:306/310 of query aligns to 9:306/311 of P0A786

query
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P0A786

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R55 (= R57) binding carbamoyl phosphate
T56 (= T58) binding carbamoyl phosphate
R106 (= R107) binding carbamoyl phosphate
H135 (= H135) binding carbamoyl phosphate
Q138 (= Q138) binding carbamoyl phosphate
L268 (= L268) binding carbamoyl phosphate
P269 (= P269) binding carbamoyl phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2ipoA

query
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2ipoA

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N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R229), L267 (= L268)

2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2h3eA

query
sites
2h3eA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R
|
R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R168), R229 (= R229), L267 (= L268)

2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2fzkA

query
sites
2fzkA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R
|
R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R
|
R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T58), H134 (= H135), Q137 (= Q138), T168 (= T169), R229 (= R229), P266 (= P267), L267 (= L268), R296 (= R297)

2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2fzgA

query
sites
2fzgA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R
|
R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S55), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R229), P266 (= P267), L267 (= L268)

2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2fzcA

query
sites
2fzcA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R

R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S55), R54 (= R57), T55 (= T58), R105 (= R107), R167 (= R168), T168 (= T169), P266 (= P267), L267 (= L268)

2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2airA

query
sites
2airA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R

R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S55), T53 (= T56), R54 (= R57), R105 (= R107)
binding phosphoric acid mono(formamide)ester: R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135)

1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 1za2A

query
sites
1za2A

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S

S

T
|
T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R

R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding phosphoric acid mono(formamide)ester: T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), R167 (= R168), T168 (= T169), L267 (= L268)

1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 1r0cA

query
sites
1r0cA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R

R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L

L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding n-carbamoyl-l-aspartate: S52 (= S55), R54 (= R57), R105 (= R107)
binding phosphate ion: R105 (= R107), H134 (= H135), Q137 (= Q138)

1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 1r0bA

query
sites
1r0bA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S
|
S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R
|
R

I

V

Q
|
Q

R

K

E

E

R

R

F

L

P

-

D

D

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L

L

P
|
P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding citrate anion: H134 (= H135), R167 (= R168), R229 (= R229), Q231 (= Q231), P266 (= P267), P268 (= P269)
binding phosphate ion: S80 (= S82), K84 (= K86)

2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2hseA

query
sites
2hseA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
|
R

T
|
T

R

R

M

L

S
|
S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R
|
R

I

V

Q
|
Q

R

K

E

E

R

R

F

L

P

A

D

-

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P
|
P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A
|
A

H

G

N

N

G
|
G

V

I

P

F

V

A

R
|
R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding aspartic acid: R54 (= R57), T55 (= T58), S58 (= S61), R105 (= R107), H134 (= H135), Q137 (= Q138), R167 (= R168), R229 (= R229), Q231 (= Q231), L267 (= L268), P268 (= P269), A289 (= A290), R296 (= R297)
binding phosphonoacetamide: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), L267 (= L268)

2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/310 of 2a0fA

query
sites
2a0fA

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
|
R

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M

L

A

A

A

T

E

E

F

F

V

S

-

G

D

N

V

V

P

P

L

V

I

L

N

N

A

A

G

G

D

D

G

G

A

S

G

N

Q

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

L

L

L

L

D

D

L

L

Y

F

T

T

M

I

R

Q

E

E

N

T

T

Q

D

G

G

R

L

L

S

D

D

N

L

L

T

H

V

V

G

A

I

M

M

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

Y

Q

A

A

L

L

T

A

K

K

F

F

D

D

A

G

-

N

R

R

Q

F

H

Y

F

F

I

I

S

A

P

P

E

D

S

A

L

L

R

A

L

M

P

P

R

Q

S

Y

V

I

R

L

Y

D

D

M

L

L

H

D

E

E

A

K

G

G

A

I

N

A

V

W

K

S

E

L

H

H

T

S

D

S

L

I

D

E

A

E

V

V

L

M

P

A

E

E

L

V

D

D

V

I

L

L

Y

Y

V

M

T
|
T

R

R

I

V

Q

Q

R

K

E

E

R

R

F

L

P

A

D

-

E

P

N

S

E

E

Y

Y

R

A

Q

N

V

V

A

K

G

A

E

Q

Y

F

R

V

I

L

D

R

A

A

A

S

G

D

L

L

D

H

A

N

A

A

R

K

D

A

D

N

L

M

T

K

L

V

M

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

D

D

E

E

I

I

A

A

P

T

D

D

V

V

D

D

G

K

S

T

Q

P

H

H

A

A

H

W

Y

Y

F

F

E

Q

Q

Q

A

A

H

G

N

N

G
|
G

V

I

P

F

V

A

R

R

M

Q

A

A

L

L

L

L

D

A

L

L

L

V

L

L

D

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T228), P266 (= P267), G292 (= G293)
binding phosphonoacetamide: R54 (= R57), T55 (= T58), H134 (= H135), Q137 (= Q138), L267 (= L268)

5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
48% identity, 96% coverage: 10:306/310 of query aligns to 8:305/309 of 5vmqC

query
sites
5vmqC

Q

H

V

I

V

I

S

S

A

I

K

N

D

D

L

L

S

S

R

R

A

D

D

D

I

L

E

N

T

L

V

V

C

L

D

A

R

T

A

A

A

A

E

K

I

L

E

K

R

A

S

N

P

P

-

Q

P

P

D

E

P

L

A

L

R

K

H

H

A

-

G

-

T

K

L

V

L

I

G

A

L

S

L

C

F

F

F

F

E

E

P

A

S

S

T

T

R
|
R

T
|
T

R

R

M

L

S

S

F

F

E

E

S

T

A

S

I

M

K

H

R

R

L

L

G

G

G

A

D

S

A

V

L

V

G

G

M

F

G

S

-

D

S

S

V

A

E

N

S

T

S

S

S

L

A

G

A

K

K
|
K

G

G

E

E

S

T

L

L

A

A

D

D

T

T

V

I

R

S

V

V

T

I

E

S

G

T

Y

Y

A

V

D

D

A

A

L

I

V

V

L

M

R
x
A

H

H

P

P

S

Q

E

E

G

G

A

A

A

A

T

R

M