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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6M8P

Human ERAP1 bound to phosphinic pseudotripeptide inhibitor DG013

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
E0008270molecular_functionzinc ion binding
F0006508biological_processproteolysis
F0008237molecular_functionmetallopeptidase activity
F0008270molecular_functionzinc ion binding
G0006508biological_processproteolysis
G0008237molecular_functionmetallopeptidase activity
G0008270molecular_functionzinc ion binding
H0006508biological_processproteolysis
H0008237molecular_functionmetallopeptidase activity
H0008270molecular_functionzinc ion binding
I0006508biological_processproteolysis
I0008237molecular_functionmetallopeptidase activity
I0008270molecular_functionzinc ion binding
J0006508biological_processproteolysis
J0008237molecular_functionmetallopeptidase activity
J0008270molecular_functionzinc ion binding
K0006508biological_processproteolysis
K0008237molecular_functionmetallopeptidase activity
K0008270molecular_functionzinc ion binding
L0006508biological_processproteolysis
L0008237molecular_functionmetallopeptidase activity
L0008270molecular_functionzinc ion binding
M0006508biological_processproteolysis
M0008237molecular_functionmetallopeptidase activity
M0008270molecular_functionzinc ion binding
N0006508biological_processproteolysis
N0008237molecular_functionmetallopeptidase activity
N0008270molecular_functionzinc ion binding
O0006508biological_processproteolysis
O0008237molecular_functionmetallopeptidase activity
O0008270molecular_functionzinc ion binding
P0006508biological_processproteolysis
P0008237molecular_functionmetallopeptidase activity
P0008270molecular_functionzinc ion binding
Q0006508biological_processproteolysis
Q0008237molecular_functionmetallopeptidase activity
Q0008270molecular_functionzinc ion binding
R0006508biological_processproteolysis
R0008237molecular_functionmetallopeptidase activity
R0008270molecular_functionzinc ion binding
S0006508biological_processproteolysis
S0008237molecular_functionmetallopeptidase activity
S0008270molecular_functionzinc ion binding
T0006508biological_processproteolysis
T0008237molecular_functionmetallopeptidase activity
T0008270molecular_functionzinc ion binding
U0006508biological_processproteolysis
U0008237molecular_functionmetallopeptidase activity
U0008270molecular_functionzinc ion binding
V0006508biological_processproteolysis
V0008237molecular_functionmetallopeptidase activity
V0008270molecular_functionzinc ion binding
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHELAHQW
ChainResidueDetails
ATHR350-TRP359
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues110
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues66
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues22
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues44
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21478864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues22
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues22
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21478864","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues22
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-21

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