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 PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE K62 A 200 |
| Chain | Residue |
| A | ASP25 |
| A | HOH135 |
| A | HOH202 |
| B | ARG8 |
| B | ASP25 |
| B | GLY27 |
| B | ALA28 |
| B | ASP30 |
| B | GLY48 |
| B | GLY49 |
| B | PRO81 |
| A | GLY27 |
| B | VAL82 |
| B | ILE84 |
| B | HOH133 |
| A | ALA28 |
| A | ASP29 |
| A | GLY48 |
| A | ILE50 |
| A | VAL82 |
| A | HOH101 |
| A | HOH120 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 501 |
| Chain | Residue |
| A | ARG14 |
| A | GLY16 |
| A | GLY17 |
| A | HOH131 |
| A | HOH144 |
| A | HOH170 |
| B | GLY16 |
| B | HOH117 |
| B | HOH176 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL |
| Chain | Residue | Details |
| A | ALA22-LEU33 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 138 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
