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 | 5 |
| Details | binding site for residue NA A 501 |
| Chain | Residue |
| A | ASP60 |
| A | HOH615 |
| A | HOH625 |
| A | HOH644 |
| A | HOH697 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | THR74 |
| A | ASN88 |
| A | HOH709 |
| A | HOH715 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue AB1 B 201 |
| Chain | Residue |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ILE47 |
| A | GLY48 |
| A | GLY49 |
| A | VAL82 |
| A | HOH652 |
| B | ARG8 |
| B | ASP25 |
| B | GLY27 |
| B | ALA28 |
| B | ASP29 |
| B | ASP30 |
| B | VAL32 |
| B | GLY48 |
| B | GLY49 |
| B | ILE50 |
| B | PRO81 |
| B | VAL82 |
| B | HOH313 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 202 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 203 |
| Chain | Residue |
| B | THR74 |
| B | ASN88 |
| B | HOH374 |
| B | HOH416 |
| B | HOH424 |
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_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 |
