6OPY
HIV-1 Protease NL4-3 I13V, G16E, V32I, L33F, K45I, M46I, A71V, L76V, V82F, I84V Mutant in complex with darunavir
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 | 19 |
Details | binding site for residue 017 A 101 |
Chain | Residue |
A | LEU23 |
A | PHE82 |
A | HOH207 |
B | ASP25 |
B | GLY27 |
B | ASP30 |
B | GLY48 |
B | GLY49 |
B | ILE50 |
B | PRO81 |
B | PHE82 |
A | ASP25 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | GLY48 |
A | GLY49 |
A | ILE50 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF |
Chain | Residue | Details |
A | ALA22-PHE33 | |
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 | |