4FKH
Crystal structure of porcine aminopeptidase-N complexed with alanine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001525 | biological_process | angiogenesis |
| A | 0001618 | molecular_function | virus receptor activity |
| A | 0002003 | biological_process | angiotensin maturation |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016285 | molecular_function | alanyl aminopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030154 | biological_process | cell differentiation |
| 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 |
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 | VAL380-TRP389 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 898 |
| Details | Region: {"description":"Metalloprotease"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Region: {"description":"Interaction with TGEV spike glycoprotein","evidences":[{"source":"PubMed","id":"7913510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8985407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634079","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22876187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F5C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22876187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F5C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
