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 |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0016020 | cellular_component | membrane |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE MV7 A 531 |
| Chain | Residue |
| A | GLY11 |
| A | TYR71 |
| A | THR72 |
| A | GLN73 |
| A | GLY74 |
| A | PHE108 |
| A | ILE110 |
| A | ILE126 |
| A | TYR198 |
| A | ASP228 |
| A | SER229 |
| A | GLN12 |
| A | GLY230 |
| A | THR231 |
| A | THR232 |
| A | ASN233 |
| A | ARG235 |
| A | SER325 |
| A | THR329 |
| A | ALA335 |
| A | GLY13 |
| A | LEU30 |
| A | ASP32 |
| A | GLY34 |
| A | SER35 |
| A | VAL69 |
| A | PRO70 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE MV7 B 531 |
| Chain | Residue |
| B | GLY11 |
| B | GLN12 |
| B | GLY13 |
| B | LEU30 |
| B | ASP32 |
| B | GLY34 |
| B | PRO70 |
| B | TYR71 |
| B | THR72 |
| B | GLN73 |
| B | GLY74 |
| B | PHE108 |
| B | ILE110 |
| B | TRP115 |
| B | ILE126 |
| B | TYR198 |
| B | LYS224 |
| B | ILE226 |
| B | ASP228 |
| B | SER229 |
| B | GLY230 |
| B | THR231 |
| B | THR232 |
| B | ASN233 |
| B | ARG235 |
| B | SER325 |
| B | THR329 |
| B | ALA335 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE MV7 C 531 |
| Chain | Residue |
| C | GLY11 |
| C | GLN12 |
| C | GLY13 |
| C | LEU30 |
| C | ASP32 |
| C | GLY34 |
| C | VAL69 |
| C | PRO70 |
| C | TYR71 |
| C | THR72 |
| C | GLN73 |
| C | GLY74 |
| C | PHE108 |
| C | ILE110 |
| C | ILE118 |
| C | ILE126 |
| C | TYR198 |
| C | LYS224 |
| C | ASP228 |
| C | SER229 |
| C | GLY230 |
| C | THR231 |
| C | THR232 |
| C | ASN233 |
| C | ARG235 |
| C | SER325 |
| C | THR329 |
| C | ALA335 |
| C | HOH428 |
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 | ILE29-VAL40 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| 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 | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
