Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ROC A 201 |
| Chain | Residue |
| A | ASP25 |
| A | PRO81 |
| A | VAL82 |
| A | ARG1008 |
| A | ASP1025 |
| A | GLY1027 |
| A | ALA1028 |
| A | ILE1047 |
| A | VAL1048 |
| A | GLY1049 |
| A | ILE1050 |
| A | GLY27 |
| A | HOH1100 |
| A | HOH1101 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | ILE47 |
| A | VAL48 |
| A | GLY49 |
| A | ILE50 |
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 | |
| A | ALA1022-LEU1033 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 69 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"PubMed","id":"2162350","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33542150","evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 175 |
| Chain | Residue | Details |
| A | ASP25 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | THR26 | electrostatic stabiliser, transition state stabiliser |
| A | GLY27 | electrostatic stabiliser, hydrogen bond donor |
