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 500 |
| Chain | Residue |
| A | ASP60 |
| A | HOH1024 |
| A | HOH1035 |
| A | HOH1066 |
| A | HOH1108 |
| A | HOH1154 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 501 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 502 |
| Chain | Residue |
| B | HOH1030 |
| B | THR174 |
| B | ASN188 |
| site_id | AC4 |
| Number of Residues | 47 |
| Details | BINDING SITE FOR CHAIN C OF PEPTIDE INHIBITOR |
| Chain | Residue |
| A | ARG8 |
| A | LEU23 |
| A | ASP25 |
| A | GLY27 |
| A | ALA28 |
| A | ASP29 |
| A | ASP30 |
| A | LYS45 |
| A | MET46 |
| A | ILE47 |
| A | GLY48 |
| A | GLY49 |
| A | ILE50 |
| A | PHE53 |
| A | PRO81 |
| A | ALA82 |
| B | ARG108 |
| B | LEU123 |
| B | ASP125 |
| B | GLY127 |
| B | ALA128 |
| B | ASP129 |
| B | ASP130 |
| B | VAL132 |
| B | LYS145 |
| B | MET146 |
| B | ILE147 |
| B | GLY148 |
| B | GLY149 |
| B | ILE150 |
| B | PHE153 |
| B | ILE184 |
| B | HOH1034 |
| B | HOH1056 |
| B | HOH1083 |
| B | HOH1128 |
| B | HOH1151 |
| B | HOH1178 |
| C | HOH1002 |
| C | HOH1010 |
| C | HOH1129 |
| C | HOH1135 |
| C | HOH1150 |
| C | HOH1160 |
| C | HOH1194 |
| C | HOH1225 |
| C | HOH1240 |
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_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"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a30 |
| Chain | Residue | Details |
| A | ASP25 | |
| A | THR26 | |
| B | THR126 | |
| B | ASP125 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a30 |
| Chain | Residue | Details |
| A | ASP25 | |
| B | ASP125 | |
