4FYR
Human aminopeptidase N (CD13) in complex with bestatin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001525 | biological_process | angiogenesis |
A | 0001618 | molecular_function | virus receptor activity |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
A | 0005886 | cellular_component | plasma membrane |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0030154 | biological_process | cell differentiation |
A | 0030667 | cellular_component | secretory granule membrane |
A | 0038023 | molecular_function | signaling receptor activity |
A | 0042277 | molecular_function | peptide binding |
A | 0043171 | biological_process | peptide catabolic process |
A | 0046718 | biological_process | symbiont entry into host cell |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
A | 0070062 | cellular_component | extracellular exosome |
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 | VAL385-TRP394 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | GLU389 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | GLY352 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT |
Chain | Residue | Details |
A | HIS388 | |
A | HIS392 | |
A | GLU411 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | TYR477 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Sulfotyrosine => ECO:0000255 |
Chain | Residue | Details |
A | TYR176 | |
A | TYR419 | |
A | TYR424 | |
A | TYR913 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | ASN128 | |
A | ASN234 | |
A | ASN681 | |
A | ASN818 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | ASN265 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22932899 |
Chain | Residue | Details |
A | ASN319 | |
A | ASN527 | |
A | ASN625 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN573 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN735 |