7P7P
Crystal structure of ERAP2 aminopeptidase in complex with phosphinic pseudotripeptide((1R)-1-Amino-3-phenylpropyl){(2S)-3-[((2S)-1-amino-1-oxo-3-phenylpropan-2-yl)amino]-2-{[3-(2-hydroxyphenyl)-isoxazol-5-yl]methyl}-3-oxopropyl}phosphinic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002250 | biological_process | adaptive immune response |
A | 0002474 | biological_process | antigen processing and presentation of peptide antigen via MHC class I |
A | 0004175 | molecular_function | endopeptidase activity |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006508 | biological_process | proteolysis |
A | 0008217 | biological_process | regulation of blood pressure |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016020 | cellular_component | membrane |
A | 0019885 | biological_process | antigen processing and presentation of endogenous peptide antigen via MHC class I |
A | 0042277 | molecular_function | peptide binding |
A | 0043171 | biological_process | peptide catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
B | 0002250 | biological_process | adaptive immune response |
B | 0002474 | biological_process | antigen processing and presentation of peptide antigen via MHC class I |
B | 0004175 | molecular_function | endopeptidase activity |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005788 | cellular_component | endoplasmic reticulum lumen |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006508 | biological_process | proteolysis |
B | 0008217 | biological_process | regulation of blood pressure |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016020 | cellular_component | membrane |
B | 0019885 | biological_process | antigen processing and presentation of endogenous peptide antigen via MHC class I |
B | 0042277 | molecular_function | peptide binding |
B | 0043171 | biological_process | peptide catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW |
Chain | Residue | Details |
A | VAL367-TRP376 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-ARG20 | |
B | MET1-ARG20 |
site_id | SWS_FT_FI2 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255 |
Chain | Residue | Details |
A | GLY21-VAL40 | |
B | GLY21-VAL40 |
site_id | SWS_FT_FI3 |
Number of Residues | 1838 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
A | PRO41-THR960 | |
B | PRO41-THR960 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22106953 |
Chain | Residue | Details |
A | GLU371 | |
B | GLU371 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22106953 |
Chain | Residue | Details |
A | GLU200 | |
B | GLU200 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY334 | |
A | HIS370 | |
A | HIS374 | |
A | GLU393 | |
B | GLY334 | |
B | HIS370 | |
B | HIS374 | |
B | GLU393 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | TYR455 | |
B | TYR455 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22106953 |
Chain | Residue | Details |
A | ASN85 | |
A | ASN219 | |
A | ASN405 | |
A | ASN650 | |
B | ASN85 | |
B | ASN219 | |
B | ASN405 | |
B | ASN650 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
Chain | Residue | Details |
A | ASN119 | |
B | ASN119 |