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 | 28 |
Details | BINDING SITE FOR RESIDUE 3TL A 200 |
Chain | Residue |
A | ARG8 |
A | GLY49 |
A | ILE50 |
A | PRO79 |
A | PRO81 |
A | VAL82 |
A | ILE84 |
A | HOH263 |
A | HOH283 |
B | ASP25 |
B | GLY27 |
A | ASP25 |
B | ALA28 |
B | ASP29 |
B | ASP30 |
B | GLY48 |
B | GLY49 |
B | ILE50 |
B | PHE53 |
B | VAL82 |
B | ILE84 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | PRO44 |
A | MET46 |
A | ILE47 |
A | GLY48 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME A 202 |
Chain | Residue |
A | VAL11 |
A | THR12 |
A | CYS67 |
A | HOH287 |
A | HOH356 |
B | LYS7 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1F1 B 201 |
Chain | Residue |
B | PRO44 |
B | LYS45 |
B | LYS55 |
B | VAL56 |
B | ARG57 |
B | THR91 |
B | GLN92 |
B | GLY94 |
B | HOH210 |
B | HOH310 |
B | HOH333 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME B 203 |
Chain | Residue |
A | LYS7 |
B | VAL11 |
B | THR12 |
B | CYS67 |
B | HOH222 |
B | HOH311 |
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
Chain | Residue | Details |
A | ASP25 | |
B | ASP25 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
B | PHE99 | |