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6Q4R

High-resolution crystal structure of ERAP1 with bound phosphinic transition-state analogue inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_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 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

222926

PDB entries from 2024-07-24

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