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 | 9 |
| Details | binding site for residue Y1 A 101 |
| Chain | Residue |
| A | GLU34 |
| A | ASP35 |
| A | GLU58 |
| A | ASP60 |
| A | Y1102 |
| A | CL103 |
| A | CL104 |
| A | HOH201 |
| A | HOH217 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue Y1 A 102 |
| Chain | Residue |
| A | GLU34 |
| A | ASP35 |
| A | GLU58 |
| A | ASP60 |
| A | Y1101 |
| A | CL103 |
| A | CL104 |
| A | HOH201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 103 |
| Chain | Residue |
| A | GLU34 |
| A | ASP35 |
| A | GLU58 |
| A | Y1101 |
| A | Y1102 |
| A | HOH217 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CL A 104 |
| Chain | Residue |
| A | GLU34 |
| A | ASP35 |
| A | GLU58 |
| A | ASP60 |
| A | Y1101 |
| A | Y1102 |
| A | HOH201 |
| A | HOH228 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 105 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 106 |
| Chain | Residue |
| A | TRP6 |
| A | HOH218 |
| B | ARG87 |
| B | ASP88 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 107 |
| Chain | Residue |
| A | ARG87 |
| A | ASP88 |
| A | HOH229 |
| B | TRP6 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | binding site for residue G04 B 201 |
| Chain | Residue |
| A | LEU23 |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASN30 |
| A | ILE32 |
| A | VAL47 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | VAL82 |
| B | ASP25 |
| B | GLY27 |
| B | ALA28 |
| B | ASP29 |
| B | ASN30 |
| B | ILE32 |
| B | VAL47 |
| B | GLY48 |
| B | GLY49 |
| B | ILE50 |
| B | VAL82 |
| B | HOH302 |
| B | HOH303 |
| B | HOH304 |
| B | HOH306 |
| B | HOH313 |
| B | HOH316 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue Y1 B 202 |
| Chain | Residue |
| B | GLU34 |
| B | ASP35 |
| B | GLU58 |
| B | ASP60 |
| B | Y1203 |
| B | CL204 |
| B | CL205 |
| B | HOH332 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue Y1 B 203 |
| Chain | Residue |
| B | GLU34 |
| B | ASP35 |
| B | GLU58 |
| B | ASP60 |
| B | Y1202 |
| B | CL204 |
| B | CL205 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 204 |
| Chain | Residue |
| B | GLU34 |
| B | ASP35 |
| B | GLU58 |
| B | Y1202 |
| B | Y1203 |
| B | HOH332 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 205 |
| Chain | Residue |
| B | GLU34 |
| B | ASP35 |
| B | GLU58 |
| B | ASP60 |
| B | Y1202 |
| B | Y1203 |
| B | HOH334 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTIF |
| Chain | Residue | Details |
| A | ALA22-PHE33 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 138 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
| 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":"12924029","evidenceCode":"ECO:0000269"}]} |
