1HVS

STRUCTURAL BASIS OF DRUG RESISTANCE FOR THE V82A MUTANT OF HIV-1 PROTEASE: BACKBONE FLEXIBILITY AND SUBSITE REPACKING

Summary for 1HVS

DescriptorHIV-1 PROTEASE, N-{1-BENZYL-(2R,3S)-2,3-DIHYDROXY-4-[3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRYLAMINO]-5-PHENYL-PENTYL}-3-METHYL-2-(3-METHYL-3-PYRIDIN-2-YLMETHYL-UREIDO)-BUTYRAMIDE (2 entities in total)
Functional Keywordshydrolase (acid protease)
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 molecular weight22346.39
Authors
Baldwin, E.T.,Bhat, T.N.,Liu, B.,Pattabiraman, N.,Erickson, J.W. (deposition date: 1994-11-17, release date: 1995-02-14, Last modification date: 2011-07-13)
Primary citation
Baldwin, E.T.,Bhat, T.N.,Liu, B.,Pattabiraman, N.,Erickson, J.W.
Structural basis of drug resistance for the V82A mutant of HIV-1 proteinase.
Nat.Struct.Biol., 2:244-249, 1995
PubMed: 7773792 (PDB entries with the same primary citation)
DOI: 10.1038/nsb0395-244
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.25 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers206.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution