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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3QNF

Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
A0002502biological_processpeptide antigen assembly with MHC class I protein complex
A0004175molecular_functionendopeptidase activity
A0004177molecular_functionaminopeptidase activity
A0005138molecular_functioninterleukin-6 receptor binding
A0005151molecular_functioninterleukin-1, type II receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006509biological_processmembrane protein ectodomain proteolysis
A0008217biological_processregulation of blood pressure
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009617biological_processresponse to bacterium
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0043171biological_processpeptide catabolic process
A0045088biological_processregulation of innate immune response
A0045444biological_processfat cell differentiation
A0045766biological_processpositive regulation of angiogenesis
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
B0001525biological_processangiogenesis
B0002250biological_processadaptive immune response
B0002376biological_processimmune system process
B0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
B0002502biological_processpeptide antigen assembly with MHC class I protein complex
B0004175molecular_functionendopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005138molecular_functioninterleukin-6 receptor binding
B0005151molecular_functioninterleukin-1, type II receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006509biological_processmembrane protein ectodomain proteolysis
B0008217biological_processregulation of blood pressure
B0008233molecular_functionpeptidase activity
B0008235molecular_functionmetalloexopeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0009617biological_processresponse to bacterium
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0043171biological_processpeptide catabolic process
B0045088biological_processregulation of innate immune response
B0045444biological_processfat cell differentiation
B0045766biological_processpositive regulation of angiogenesis
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
C0001525biological_processangiogenesis
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
C0002502biological_processpeptide antigen assembly with MHC class I protein complex
C0004175molecular_functionendopeptidase activity
C0004177molecular_functionaminopeptidase activity
C0005138molecular_functioninterleukin-6 receptor binding
C0005151molecular_functioninterleukin-1, type II receptor binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0006509biological_processmembrane protein ectodomain proteolysis
C0008217biological_processregulation of blood pressure
C0008233molecular_functionpeptidase activity
C0008235molecular_functionmetalloexopeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0009617biological_processresponse to bacterium
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
C0043171biological_processpeptide catabolic process
C0045088biological_processregulation of innate immune response
C0045444biological_processfat cell differentiation
C0045766biological_processpositive regulation of angiogenesis
C0046872molecular_functionmetal ion binding
C0070006molecular_functionmetalloaminopeptidase activity
C0070062cellular_componentextracellular exosome
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 Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
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 Residues3
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 Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21478864","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-07-09

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