1RPI
Crystal structures of a Multidrug-Resistant HIV-1 Protease Reveal an Expanded Active Site Cavity
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0044174 | cellular_component | host cell endosome |
A | 0055036 | cellular_component | virion membrane |
A | 0072494 | cellular_component | host multivesicular body |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0044174 | cellular_component | host cell endosome |
B | 0055036 | cellular_component | virion membrane |
B | 0072494 | cellular_component | host multivesicular body |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASN25 | |
A | THR26 | |
B | ASN25 | |
B | THR26 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASN25 | |
B | ASN25 |