2AVS

kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S

Summary for 2AVS

• Entry DOI: 10.2210/pdb2avs/pdb
• Descriptor: Pol polyprotein, PHOSPHATE ION, SULFATE ION, ... (7 entities in total)
• Functional Keywords: drug resistance, hiv-1 protease, indinavir, substrate analog, non-active site mutants., hydrolase
• 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): P04587
• Total number of polymer chains: 2
• Total formula weight: 22671.43

Authors

Liu, F.,Boross, P.I.,Wang, Y.F.,Tozser, J.,Louis, J.M.,Harrison, R.W.,Weber, I.T. (deposition date: 2005-08-30, release date: 2006-01-24, Last modification date: 2023-08-23)

• Primary citation: Liu, F.,Boross, P.I.,Wang, Y.F.,Tozser, J.,Louis, J.M.,Harrison, R.W.,Weber, I.T.; Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S.; J.Mol.Biol., 354:789-800, 2005; PubMed: 16277992; DOI: 10.1016/j.jmb.2005.09.095

Experimental method

X-RAY DIFFRACTION (1.1 Å)