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 |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 911 |
| Chain | Residue |
| A | THR74 |
| A | ASN88 |
| D | ARG41 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 921 |
| Chain | Residue |
| A | LYS45 |
| A | MET46 |
| A | ILE47 |
| B | GLN61 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ROC B 801 |
| Chain | Residue |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | THR80 |
| A | PRO81 |
| A | ILE84 |
| B | ARG8 |
| B | ASP25 |
| B | GLY27 |
| B | ASP29 |
| B | ASP30 |
| B | ILE47 |
| B | GLY48 |
| B | GLY49 |
| B | ILE50 |
| B | THR80 |
| B | PRO81 |
| B | ILE84 |
| A | TRP6 |
| A | ARG8 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 913 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ROC C 901 |
| Chain | Residue |
| C | TRP6 |
| C | ARG8 |
| C | ASP25 |
| C | GLY27 |
| C | ALA28 |
| C | ASP29 |
| C | ASP30 |
| C | ILE47 |
| C | GLY48 |
| C | GLY49 |
| C | ILE50 |
| C | THR80 |
| C | ILE84 |
| C | HOH1004 |
| C | HOH1010 |
| D | ARG8 |
| D | ASP25 |
| D | GLY27 |
| D | ASP29 |
| D | ASP30 |
| D | ILE47 |
| D | GLY48 |
| D | GLY49 |
| D | ILE50 |
| D | PRO81 |
| D | ILE84 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 912 |
| Chain | Residue |
| B | ARG41 |
| C | THR74 |
| C | ASN88 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 914 |
| Chain | Residue |
| D | GLY73 |
| D | THR74 |
| D | ASN88 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI |
| Chain | Residue | Details |
| A | ALA22-ILE33 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 276 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]} |
