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 | 6 |
| Details | binding site for residue NA A 501 |
| Chain | Residue |
| A | ASP60 |
| A | HOH608 |
| A | HOH632 |
| A | HOH646 |
| A | HOH662 |
| A | HOH680 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | THR74 |
| A | ASN88 |
| A | HOH695 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | GLN18 |
| A | SER37 |
| A | HOH688 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | LYS45 |
| A | MET46 |
| A | HOH604 |
| A | HOH641 |
| A | HOH655 |
| site_id | AC5 |
| Number of Residues | 37 |
| Details | binding site for residue TPV B 201 |
| Chain | Residue |
| A | ARG8 |
| A | LEU23 |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | ILE47 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | PRO81 |
| A | VAL82 |
| A | HOH601 |
| A | HOH614 |
| A | HOH620 |
| A | HOH641 |
| A | HOH642 |
| B | ARG8 |
| B | LEU23 |
| B | ASP25 |
| B | GLY27 |
| B | ALA28 |
| B | ASP29 |
| B | ASP30 |
| B | ILE47 |
| B | GLY48 |
| B | GLY49 |
| B | ILE50 |
| B | PRO81 |
| B | VAL82 |
| B | ILE84 |
| B | GOL203 |
| B | HOH312 |
| B | HOH317 |
| B | HOH331 |
| B | HOH402 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| B | THR74 |
| B | ASN88 |
| B | HOH333 |
| B | HOH397 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 203 |
| Chain | Residue |
| B | ALA28 |
| B | ASP29 |
| B | ILE47 |
| B | GLY48 |
| B | TPV201 |
| B | HOH317 |
| B | HOH322 |
| B | HOH331 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 204 |
| Chain | Residue |
| A | LEU5 |
| A | TRP6 |
| B | ARG87 |
| B | ASN88 |
| B | THR91 |
| B | HOH301 |
| B | HOH307 |
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 |
