SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_048042521.1 NCBI__GCF_000007065.1:WP_048042521.1 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)
57% identity, 99% coverage: 3:307/308 of query aligns to 2:307/307 of 1ml4A

query
sites
1ml4A

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

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
59% identity, 96% coverage: 6:300/308 of query aligns to 2:296/304 of 4eknB

query
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4eknB

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active site: T225 (= T227), P262 (= P266), G288 (= G292)
binding sulfate ion: G163 (= G166), R164 (= R167), T165 (= T168), R226 (= R228)

P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
49% identity, 97% coverage: 6:305/308 of query aligns to 8:306/311 of P0A786

query
sites
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 (= L267) binding carbamoyl phosphate
P269 (= P268) 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)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2ipoA

query
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2ipoA

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G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R167), T168 (= T168), R229 (= R228), L267 (= L267)

2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2h3eA

query
sites
2h3eA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R167), R229 (= R228), L267 (= L267)

2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2fzkA

query
sites
2fzkA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R
|
R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T58), H134 (= H135), Q137 (= Q138), T168 (= T168), R229 (= R228), P266 (= P266), L267 (= L267), R296 (= R296)

2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2fzgA

query
sites
2fzgA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S55), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), R167 (= R167), T168 (= T168), R229 (= R228), P266 (= P266), L267 (= L267)

2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2fzcA

query
sites
2fzcA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S55), R54 (= R57), T55 (= T58), R105 (= R107), R167 (= R167), T168 (= T168), P266 (= P266), L267 (= L267)

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)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2at1A

query
sites
2at1A

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

Q

-

T

E

E

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

E

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding alpha-D-glucopyranose: R167 (= R167), R229 (= R228)
binding phosphonoacetamide: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), Q137 (= Q138)

2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 2airA

query
sites
2airA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
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)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 1za2A

query
sites
1za2A

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L
|
L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding phosphoric acid mono(formamide)ester: T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), R167 (= R167), T168 (= T168), L267 (= L267)

1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 1r0cA

query
sites
1r0cA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
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)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 1r0bA

query
sites
1r0bA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S
|
S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

E

-

T

E

Q

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

Q

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L

L

P
|
P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding citrate anion: H134 (= H135), R167 (= R167), R229 (= R228), Q231 (= Q230), P266 (= P266), P268 (= P268)
binding phosphate ion: S80 (= S82), K84 (= K86)

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)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 1at1A

query
sites
1at1A

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

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

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E

N

T

L

L

A

A

D

D

T

T

I

I

R

S

V

V

I

I

S

S

K

T

Y

Y

A

V

D

D

L

A

I

I

V

V

L

M

R
|
R

H

H

P

P

L

Q

D

E

G

G

S

A

A

A

R

R

M

L

A

A

T

T

E

E

F

F

A

S

A

G

-

N

V

V

P

P

V

V

I

L

N

N

G

A

G

G

D

D

G

G

S

S

V

N

H

Q

H
|
H

P

P

T

T

Q
|
Q

T

T

F

L

L

L

D

D

L

L

Y

F

T

T

I

I

R

Q

R

Q

-

T

E

E

S

G

H

R

L

L

E

D

G

N

L

L

K

H

I

V

A

A

M

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

C

T

Y

Q

A

A

L

L

S

A

L

K

Y

F

-

D

G

G

A

N

E

R

M

F

T

Y

F

F

V

I

S

A

P

P

P

D

E

A

L

L

R

A

M

M

P

P

R

E

E

Y

I

I

V

L

R

D

E

M

L

L

R

D

K

E

K

K

N

G

I

I

R

A

V

W

K

S

E

L

S

H

E

S

C

S

L

I

E

E

E

E

I

V

I

M

G

A

D

E

I

V

E

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

P

-

D

D

P

P

Q

S

E

E

Y

Y

E

A

K

N

V

V

K

K

N

A

K

Q

L

F

K

V

I

L

T

R

G

A

D

S

L

D

L

L

K

H

S

N

A

A

D

K

P

A

E

N

L

M

K

K

I

V

L

L

H

H

P
|
P

L

L

P

P

R

R

V

V

N

D

E

E

I

I

S

A

P

T

D

D

V

V

D

D

D

K

T

T

P

P

H

H

A

A

R

W

Y

Y

F

F

E

Q

Q

Q

A

A

F

G

Y

N

G
|
G

V

I

P

F

I

A

R

R

M

Q

A

A

L

L

L

L

A

A

L

L

T

V

I

L

G

N

active site: R54 (= R57), T55 (= T58), K84 (= K86), R105 (= R107), H134 (= H135), Q137 (= Q138), T228 (= T227), P266 (= P266), G292 (= G292)
binding malonate ion: H134 (= H135), R167 (= R167), R229 (= R228), Q231 (= Q230)
binding phosphonoacetamide: S52 (= S55), T53 (= T56), R54 (= R57), T55 (= T58), R105 (= R107), H134 (= H135), Q137 (= Q138)

1acmA Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, nmr and x-ray crystallography study (see paper)
49% identity, 97% coverage: 6:305/308 of query aligns to 7:305/310 of 1acmA

query
sites
1acmA

R

K

H

H

V

I

I

I

S

S

M

I

K

N

D

D

F

L

S

S

R

R

E

D

E

D

I

L

D

N

Y

L

I

V

L

L

D

A

I

T

A

A

E

A

K

K

L

L

E

-

P

-

V

-

A

-

R

K

G

A

E

N

E

P

R

Q

S

P

R

E

L

L

L

L

D

K

G

H

K

K

I

V

I

I

S

A

L

S

L

C

F

F

F

F

E

E

P

A

S
|
S

T
|
T

R
x
A

T
|
T

R

R

L

L

S

S

F

F

E

Q

V

T

A

S

T

M

R

H

R

R

L

L

G

G

G

A

Q

S

V

V

L

V

S

G

L

F

G

S

-

D

S

S

V

A

E

N

A

T

S

S

S

L

V

G

M

K

K
|
K

G

G

E

E