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 4Q1Y

Related4Q1W 4Q1X
Descriptoraspartyl protease, PHOSPHATE ION, ACETATE ION, ... (5 entities in total)
Functional Keywordshiv-1 protease, aids, inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Total number of polymer chains2
Total molecular weight22737.38
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

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.208110.5%0.6%5.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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