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; PubMed: 21446746; DOI: 10.1021/bi200033z

Experimental method

X-RAY DIFFRACTION (1.45 Å)