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TitleRevertant mutation V48G alters conformational dynamics of highly drug resistant HIV protease PRS17.
Journal, issue, pagesJ. Mol. Graph. Model., Vol. 108, Page 108005-108005, Year 2021
Publish dateJun 9, 2021 (structure data deposition date)
AuthorsBurnaman, S.H. / Kneller, D.W. / Wang, Y.F. / Kovalevsky, A. / Weber, I.T.
External linksJ. Mol. Graph. Model. / PubMed:34419931
MethodsX-ray diffraction
Resolution1.32 - 1.47 Å
Structure data

PDB-7n6t:
Crystal structure of inhibitor-free HIV-1 PRS17 revertant mutant PRS17 V48G
Method: X-RAY DIFFRACTION / Resolution: 1.32 Å

PDB-7n6v:
Crystal structure of HIV-1 Protease multiple mutants PRS17 with Revertant mutation V48G bound to inhibitor Amprenavir
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

PDB-7n6x:
Crystal structure of HIV-1 Protease multiple mutants PRS17 bound to inhibitor Amprenavir
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-478:
{3-[(4-AMINO-BENZENESULFONYL)-ISOBUTYL-AMINO]-1-BENZYL-2-HYDROXY-PROPYL}-CARBAMIC ACID TETRAHYDRO-FURAN-3-YL ESTER / protease inhibitor, medication*YM

ChemComp-GOL:
GLYCEROL

Source
  • human immunodeficiency virus type 1 group m subtype b (isolate bru/lai)
KeywordsHYDROLASE / HIV-1 Protease / drug resistance / PRS17

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