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TitleComparing the Accumulation of Active- and Nonactive-Site Mutations in the HIV-1 Protease.
Journal, issue, pagesBiochemistry, Vol. 43, Page 12141-12151, Year 2004
Publish dateFeb 24, 2004 (structure data deposition date)
AuthorsClemente, 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.
External linksBiochemistry / PubMed:15379553
MethodsX-ray diffraction
Resolution1.9 - 2.5 Å
Structure data

PDB-1sgu:
Comparing the Accumulation of Active Site and Non-active Site Mutations in the HIV-1 Protease
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1sh9:
Comparing the Accumulation of Active Site and Non-active Site Mutations in the HIV-1 Protease
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-MK1:
N-[2(R)-HYDROXY-1(S)-INDANYL]-5-[(2(S)-TERTIARY / antivirus, antiretroviral, protease inhibitor, medication*YM

ChemComp-HOH:
WATER

ChemComp-RIT:
RITONAVIR

Source
  • human immunodeficiency virus 1
KeywordsHYDROLASE / ACTIVE SITE MUTATIONS / NON-ACTIVE SITE MUTATIONS / INDINAVIR / HIV-1 PROTEASE / HYDROLASE/HYDROLASE INHIBITOR / ritonavir / HYDROLASE-HYDROLASE INHIBITOR complex

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