3PWM

HIV-1 Protease Mutant L76V with Darunavir

Summary for 3PWM

Entry DOI	10.2210/pdb3pwm/pdb
Related	2IEN 3PWR
Descriptor	Protease, CHLORIDE ION, ACETATE ION, ... (6 entities in total)
Functional Keywords	hiv-1, protease, mutation l76v, darunavir, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Human immunodeficiency virus 1
Cellular location	Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03367
Total number of polymer chains	2
Total formula weight	22271.99
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: 21446746 DOI: 10.1021/bi200033z PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.46 Å)

Structure validation