Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI A 501 |
Chain | Residue |
A | GLU316 |
A | ASP451 |
A | HIS457 |
A | HIS459 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 3UY A 502 |
Chain | Residue |
A | GLY95 |
A | TYR132 |
A | PHE169 |
A | ILE171 |
A | ILE179 |
A | ASP289 |
A | GLY291 |
A | HOH618 |
A | HOH829 |
A | GLY72 |
A | GLN73 |
A | GLY74 |
A | LEU91 |
A | ASP93 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV |
Chain | Residue | Details |
A | ILE90-VAL101 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |