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2AVM

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

Summary for 2AVM
Entry DOI10.2210/pdb2avm/pdb
Related2AVO 2AVQ 2AVS 2AVV
Related PRD IDPRD_000398
DescriptorHIV-1 protease, GLYCEROL, N-{(2S)-2-[(N-acetyl-L-threonyl-L-isoleucyl)amino]hexyl}-L-norleucyl-L-glutaminyl-N~5~-[amino(iminio)methyl]-L-ornithinamide, ... (5 entities in total)
Functional Keywordshiv-1 protease, drug resistance, substrate analog, non-active site mutants, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationMatrix 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 chains2
Total formula weight22588.67
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: 2024-03-13)
Primary citationLiu, 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
Cited by
PubMed: 16277992
DOI: 10.1016/j.jmb.2005.09.095
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.1 Å)
Structure validation

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