Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNVWV |
| Chain | Residue | Details |
| A | VAL35-VAL46 | |
| A | ALA223-GLY234 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"20927107","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"2493678","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 317 |
| Details | Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]} |
