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TitleStructural Basis of Why Nelfinavir-Resistant D30N Mutant of HIV-1 Protease Remains Susceptible to Saquinavir.
Journal, issue, pagesChem. Biol. Drug Des., Vol. 86, Page 302-308, Year 2015
Publish dateApr 17, 2014 (structure data deposition date)
AuthorsPrashar, V. / Bihani, S.C. / Ferrer, J.L. / Hosur, M.V.
External linksChem. Biol. Drug Des. / PubMed:25487655
MethodsX-ray diffraction
Resolution1.795 Å
Structure data

PDB-4q5m:
D30N tethered HIV-1 protease dimer/saquinavir complex
Method: X-RAY DIFFRACTION / Resolution: 1.795 Å

Chemicals

ChemComp-ROC:
(2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus type 1
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR complex

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