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 | 20 |
Details | BINDING SITE FOR RESIDUE L27 A 479 |
Chain | Residue |
A | ASP25 |
B | ASP225 |
B | GLY227 |
B | ALA228 |
B | ASP229 |
B | ASP230 |
B | GLY248 |
B | GLY249 |
B | ILE250 |
B | PRO281 |
B | VAL282 |
A | GLY27 |
B | ILE284 |
A | ASP30 |
A | VAL32 |
A | GLY48 |
A | GLY49 |
A | HOH489 |
B | HOH50 |
B | LEU223 |
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 | ASP225 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | ILE64 | |
B | ILE264 | |
Chain | Residue | Details |
A | PHE99 | |
B | PHE299 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by host => ECO:0000250 |
Chain | Residue | Details |
A | ILE64 | |
B | ILE264 | |
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 | THR226 | |
B | ASP225 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
B | ASP225 | |