1SH9

Comparing the Accumulation of Active Site and Non-active Site Mutations in the HIV-1 Protease

Summary for 1SH9

Related1SGU
Related PRD IDPRD_001001
DescriptorPOL polyprotein, RITONAVIR (3 entities in total)
Functional Keywordshiv-1 protease, non-active site mutations, active site mutations, ritonavir, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationGag-Pol polyprotein: Host cell membrane ; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion  P03367
Total number of polymer chains2
Total molecular weight22392.38
Authors
Clemente, J.C.,Moose, R.E.,Hemrajani, R.,Govindasamy, L.,Reutzel, R.,McKenna, R.,Abanje-McKenna, M.,Goodenow, M.M.,Dunn, B.M. (deposition date: 2004-02-25, release date: 2004-10-05, Last modification date: 2017-10-11)
Primary citation
Clemente, J.C.,Moose, R.E.,Hemrajani, R.,Whitford, L.R.,Govindasamy, L.,Reutzel, R.,McKenna, R.,Agbandje-McKenna, M.,Goodenow, M.M.,Dunn, B.M.
Comparing the Accumulation of Active- and Nonactive-Site Mutations in the HIV-1 Protease.
Biochemistry, 43:12141-12151, 2004
PubMed: 15379553 (PDB entries with the same primary citation)
DOI: 10.1021/bi049459m
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.5 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.274281.0%3.6%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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