4Q1W

Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance

Summary for 4Q1W

Related4Q1X 4Q1Y
DescriptorASPARTYL PROTEASE, PHOSPHATE ION, (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE, ... (5 entities in total)
Functional Keywordshiv-1 protease, aids, inhibitor complex, aspartyl protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Total number of polymer chains2
Total molecular weight22654.25
Authors
Ragland, D.A.,Nalam, M.N.L.,Cao, H.,Nalivaika, E.A.,Cai, Y.,Kurt-Yilmaz, N.,Schiffer, C.A. (deposition date: 2014-04-04, release date: 2015-02-18)
Primary citation
Ragland, D.A.,Nalivaika, E.A.,Nalam, M.N.,Prachanronarong, K.L.,Cao, H.,Bandaranayake, R.M.,Cai, Y.,Kurt-Yilmaz, N.,Schiffer, C.A.
Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease.
J.Am.Chem.Soc., 136:11956-11963, 2014
PubMed: 25091085 (PDB entries with the same primary citation)
DOI: 10.1021/ja504096m
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.85 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.220300.6%1.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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