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6RQX

High-resolution crystal structure of ERAP1 in complex with 10mer phosphinic peptide

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
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
A0042277molecular_functionpeptide binding
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
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 Residues1
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
AVAL2-LEU21

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU354

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU183
AGLY317

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS353
AHIS357
AGLU376

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
ATYR438

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16
ChainResidueDetails
AASN70
AASN154

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|Ref.16
ChainResidueDetails
AASN414

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21478864
ChainResidueDetails
AASN760

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN901

218853

PDB entries from 2024-04-24

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