3PWR
HIV-1 Protease Mutant L76V complexed with Saquinavir
Summary for 3PWR
Entry DOI | 10.2210/pdb3pwr/pdb |
Related | 3OXC |
Related PRD ID | PRD_000454 |
Descriptor | Protease, (2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 -phenyl-butan-2-yl]-2-(quinolin-2-ylcarbonylamino)butanediamide, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | hiv-1, protease, mutation l76v, saquinavir, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Human immunodeficiency virus 1 |
Cellular location | Gag-Pol polyprotein: Host cell membrane ; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03367 |
Total number of polymer chains | 2 |
Total formula weight | 22896.35 |
Authors | Zhang, Y.,Weber, I.T. (deposition date: 2010-12-08, release date: 2011-04-20, Last modification date: 2023-09-13) |
Primary citation | Louis, J.M.,Zhang, Y.,Sayer, J.M.,Wang, Y.F.,Harrison, R.W.,Weber, I.T. The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts. Biochemistry, 50:4786-4795, 2011 Cited by PubMed: 21446746DOI: 10.1021/bi200033z PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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