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 | 21 |
Details | binding site for residue 017 B 201 |
Chain | Residue |
A | ASP25 |
B | ASP25 |
B | GLY27 |
B | ALA28 |
B | ASP30 |
B | ILE32 |
B | GLY48 |
B | GLY49 |
B | PRO81 |
B | ILE82 |
B | DOD307 |
A | GLY27 |
B | DOD315 |
B | DOD326 |
A | ASP29 |
A | ASP30 |
A | ILE32 |
A | VAL47 |
A | GLY48 |
A | ILE50 |
A | ILE84 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII |
Chain | Residue | Details |
A | ALA22-ILE33 | |
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 | |