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 | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 101 |
| Chain | Residue |
| A | ARG14 |
| A | GLY16 |
| A | GLY17 |
| A | HOH247 |
| B | GLY16 |
| B | HOH208 |
| B | HOH221 |
| B | HOH233 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 102 |
| Chain | Residue |
| A | GLU21 |
| A | HOH239 |
| B | HOH230 |
| A | LYS20 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 103 |
| Chain | Residue |
| A | MET36 |
| A | ASN37 |
| A | HOH249 |
| B | PRO39 |
| B | GLY40 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 017 A 104 |
| Chain | Residue |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | HOH206 |
| B | ASP25 |
| B | GLY27 |
| B | ALA28 |
| B | ASP30 |
| B | GLY48 |
| B | GLY49 |
| B | PRO81 |
| B | VAL82 |
| B | HOH239 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 101 |
| Chain | Residue |
| A | ARG87 |
| B | TRP6 |
| B | LYS7 |
| B | ARG8 |
| B | HOH232 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 102 |
| Chain | Residue |
| A | GLY49 |
| A | HOH220 |
| B | THR91 |
| B | GLN92 |
| B | HOH255 |
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_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"PubMed","id":"2162350","evidenceCode":"ECO:0000269"}]} |
| 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"},{"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 |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 175 |
| Chain | Residue | Details |
| B | ASP25 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | THR26 | electrostatic stabiliser, transition state stabiliser |
| B | GLY27 | electrostatic stabiliser, hydrogen bond donor |
