6M8P
Human ERAP1 bound to phosphinic pseudotripeptide inhibitor DG013
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
D | 0006508 | biological_process | proteolysis |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0008270 | molecular_function | zinc ion binding |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008270 | molecular_function | zinc ion binding |
F | 0006508 | biological_process | proteolysis |
F | 0008237 | molecular_function | metallopeptidase activity |
F | 0008270 | molecular_function | zinc ion binding |
G | 0006508 | biological_process | proteolysis |
G | 0008237 | molecular_function | metallopeptidase activity |
G | 0008270 | molecular_function | zinc ion binding |
H | 0006508 | biological_process | proteolysis |
H | 0008237 | molecular_function | metallopeptidase activity |
H | 0008270 | molecular_function | zinc ion binding |
I | 0006508 | biological_process | proteolysis |
I | 0008237 | molecular_function | metallopeptidase activity |
I | 0008270 | molecular_function | zinc ion binding |
J | 0006508 | biological_process | proteolysis |
J | 0008237 | molecular_function | metallopeptidase activity |
J | 0008270 | molecular_function | zinc ion binding |
K | 0006508 | biological_process | proteolysis |
K | 0008237 | molecular_function | metallopeptidase activity |
K | 0008270 | molecular_function | zinc ion binding |
L | 0006508 | biological_process | proteolysis |
L | 0008237 | molecular_function | metallopeptidase activity |
L | 0008270 | molecular_function | zinc ion binding |
M | 0006508 | biological_process | proteolysis |
M | 0008237 | molecular_function | metallopeptidase activity |
M | 0008270 | molecular_function | zinc ion binding |
N | 0006508 | biological_process | proteolysis |
N | 0008237 | molecular_function | metallopeptidase activity |
N | 0008270 | molecular_function | zinc ion binding |
O | 0006508 | biological_process | proteolysis |
O | 0008237 | molecular_function | metallopeptidase activity |
O | 0008270 | molecular_function | zinc ion binding |
P | 0006508 | biological_process | proteolysis |
P | 0008237 | molecular_function | metallopeptidase activity |
P | 0008270 | molecular_function | zinc ion binding |
Q | 0006508 | biological_process | proteolysis |
Q | 0008237 | molecular_function | metallopeptidase activity |
Q | 0008270 | molecular_function | zinc ion binding |
R | 0006508 | biological_process | proteolysis |
R | 0008237 | molecular_function | metallopeptidase activity |
R | 0008270 | molecular_function | zinc ion binding |
S | 0006508 | biological_process | proteolysis |
S | 0008237 | molecular_function | metallopeptidase activity |
S | 0008270 | molecular_function | zinc ion binding |
T | 0006508 | biological_process | proteolysis |
T | 0008237 | molecular_function | metallopeptidase activity |
T | 0008270 | molecular_function | zinc ion binding |
U | 0006508 | biological_process | proteolysis |
U | 0008237 | molecular_function | metallopeptidase activity |
U | 0008270 | molecular_function | zinc ion binding |
V | 0006508 | biological_process | proteolysis |
V | 0008237 | molecular_function | metallopeptidase activity |
V | 0008270 | molecular_function | zinc ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHELAHQW |
Chain | Residue | Details |
A | THR350-TRP359 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095 |
Chain | Residue | Details |
A | GLU354 | |
J | GLU354 | |
K | GLU354 | |
L | GLU354 | |
M | GLU354 | |
N | GLU354 | |
O | GLU354 | |
P | GLU354 | |
Q | GLU354 | |
R | GLU354 | |
S | GLU354 | |
B | GLU354 | |
T | GLU354 | |
U | GLU354 | |
V | GLU354 | |
C | GLU354 | |
D | GLU354 | |
E | GLU354 | |
F | GLU354 | |
G | GLU354 | |
H | GLU354 | |
I | GLU354 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU183 | |
E | GLY317 | |
F | GLU183 | |
F | GLY317 | |
G | GLU183 | |
G | GLY317 | |
H | GLU183 | |
H | GLY317 | |
I | GLU183 | |
I | GLY317 | |
J | GLU183 | |
A | GLY317 | |
J | GLY317 | |
K | GLU183 | |
K | GLY317 | |
L | GLU183 | |
L | GLY317 | |
M | GLU183 | |
M | GLY317 | |
N | GLU183 | |
N | GLY317 | |
O | GLU183 | |
B | GLU183 | |
O | GLY317 | |
P | GLU183 | |
P | GLY317 | |
Q | GLU183 | |
Q | GLY317 | |
R | GLU183 | |
R | GLY317 | |
S | GLU183 | |
S | GLY317 | |
T | GLU183 | |
B | GLY317 | |
T | GLY317 | |
U | GLU183 | |
U | GLY317 | |
V | GLU183 | |
V | GLY317 | |
C | GLU183 | |
C | GLY317 | |
D | GLU183 | |
D | GLY317 | |
E | GLU183 |
site_id | SWS_FT_FI3 |
Number of Residues | 66 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS353 | |
D | HIS353 | |
D | HIS357 | |
D | GLU376 | |
E | HIS353 | |
E | HIS357 | |
E | GLU376 | |
F | HIS353 | |
F | HIS357 | |
F | GLU376 | |
G | HIS353 | |
A | HIS357 | |
G | HIS357 | |
G | GLU376 | |
H | HIS353 | |
H | HIS357 | |
H | GLU376 | |
I | HIS353 | |
I | HIS357 | |
I | GLU376 | |
J | HIS353 | |
J | HIS357 | |
A | GLU376 | |
J | GLU376 | |
K | HIS353 | |
K | HIS357 | |
K | GLU376 | |
L | HIS353 | |
L | HIS357 | |
L | GLU376 | |
M | HIS353 | |
M | HIS357 | |
M | GLU376 | |
B | HIS353 | |
N | HIS353 | |
N | HIS357 | |
N | GLU376 | |
O | HIS353 | |
O | HIS357 | |
O | GLU376 | |
P | HIS353 | |
P | HIS357 | |
P | GLU376 | |
Q | HIS353 | |
B | HIS357 | |
Q | HIS357 | |
Q | GLU376 | |
R | HIS353 | |
R | HIS357 | |
R | GLU376 | |
S | HIS353 | |
S | HIS357 | |
S | GLU376 | |
T | HIS353 | |
T | HIS357 | |
B | GLU376 | |
T | GLU376 | |
U | HIS353 | |
U | HIS357 | |
U | GLU376 | |
V | HIS353 | |
V | HIS357 | |
V | GLU376 | |
C | HIS353 | |
C | HIS357 | |
C | GLU376 |
site_id | SWS_FT_FI4 |
Number of Residues | 22 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | TYR438 | |
J | TYR438 | |
K | TYR438 | |
L | TYR438 | |
M | TYR438 | |
N | TYR438 | |
O | TYR438 | |
P | TYR438 | |
Q | TYR438 | |
R | TYR438 | |
S | TYR438 | |
B | TYR438 | |
T | TYR438 | |
U | TYR438 | |
V | TYR438 | |
C | TYR438 | |
D | TYR438 | |
E | TYR438 | |
F | TYR438 | |
G | TYR438 | |
H | TYR438 | |
I | TYR438 |
site_id | SWS_FT_FI5 |
Number of Residues | 44 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16 |
Chain | Residue | Details |
A | ASN70 | |
E | ASN154 | |
F | ASN70 | |
F | ASN154 | |
G | ASN70 | |
G | ASN154 | |
H | ASN70 | |
H | ASN154 | |
I | ASN70 | |
I | ASN154 | |
J | ASN70 | |
A | ASN154 | |
J | ASN154 | |
K | ASN70 | |
K | ASN154 | |
L | ASN70 | |
L | ASN154 | |
M | ASN70 | |
M | ASN154 | |
N | ASN70 | |
N | ASN154 | |
O | ASN70 | |
B | ASN70 | |
O | ASN154 | |
P | ASN70 | |
P | ASN154 | |
Q | ASN70 | |
Q | ASN154 | |
R | ASN70 | |
R | ASN154 | |
S | ASN70 | |
S | ASN154 | |
T | ASN70 | |
B | ASN154 | |
T | ASN154 | |
U | ASN70 | |
U | ASN154 | |
V | ASN70 | |
V | ASN154 | |
C | ASN70 | |
C | ASN154 | |
D | ASN70 | |
D | ASN154 | |
E | ASN70 |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|Ref.16 |
Chain | Residue | Details |
A | ASN414 | |
J | ASN414 | |
K | ASN414 | |
L | ASN414 | |
M | ASN414 | |
N | ASN414 | |
O | ASN414 | |
P | ASN414 | |
Q | ASN414 | |
R | ASN414 | |
S | ASN414 | |
B | ASN414 | |
T | ASN414 | |
U | ASN414 | |
V | ASN414 | |
C | ASN414 | |
D | ASN414 | |
E | ASN414 | |
F | ASN414 | |
G | ASN414 | |
H | ASN414 | |
I | ASN414 |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21478864 |
Chain | Residue | Details |
A | ASN735 | |
J | ASN735 | |
K | ASN735 | |
L | ASN735 | |
M | ASN735 | |
N | ASN735 | |
O | ASN735 | |
P | ASN735 | |
Q | ASN735 | |
R | ASN735 | |
S | ASN735 | |
B | ASN735 | |
T | ASN735 | |
U | ASN735 | |
V | ASN735 | |
C | ASN735 | |
D | ASN735 | |
E | ASN735 | |
F | ASN735 | |
G | ASN735 | |
H | ASN735 | |
I | ASN735 |
site_id | SWS_FT_FI8 |
Number of Residues | 22 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN876 | |
J | ASN876 | |
K | ASN876 | |
L | ASN876 | |
M | ASN876 | |
N | ASN876 | |
O | ASN876 | |
P | ASN876 | |
Q | ASN876 | |
R | ASN876 | |
S | ASN876 | |
B | ASN876 | |
T | ASN876 | |
U | ASN876 | |
V | ASN876 | |
C | ASN876 | |
D | ASN876 | |
E | ASN876 | |
F | ASN876 | |
G | ASN876 | |
H | ASN876 | |
I | ASN876 |