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Structure paper

TitleCrystal Structures of Highly Constrained Substrate and Hydrolysis Products Bound to HIV-1 Protease. Implications for the Catalytic Mechanism
Journal, issue, pagesBiochemistry, Vol. 47, Page 3736-3744, Year 2008
Publish dateJan 14, 2008 (structure data deposition date)
AuthorsTyndall, J.D. / Pattenden, L.K. / Reid, R.C. / Hu, S.H. / Alewood, D. / Alewood, P.F. / Walsh, T. / Fairlie, D.P. / Martin, J.L.
External linksBiochemistry / PubMed:18311928
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-3bxr:
Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1 Protease. Implications For Catalytic Mechanism
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3bxs:
Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1 Protease. Implications For Catalytic Mechanism
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-DRR:
(9S,12S)-9-(1-methylethyl)-N-[(8S,11S)-8-[(1S)-1-methylpropyl]-7,10-dioxo-2-oxa-6,9-diazabicyclo[11.2.2]heptadeca-1(15),13,16-trien-11-yl]-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxamide

ChemComp-HOH:
WATER

ChemComp-DRS:
(9S,12S)-9-(1-methylethyl)-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxylic acid

KeywordsHYDROLASE / HIV protease / HIVPR / substrate / product / AIDS / Aspartyl protease / Capsid maturation / Core protein / Cytoplasm / DNA integration / DNA recombination / DNA-directed DNA polymerase / Endonuclease / Lipoprotein / Magnesium / Membrane / Metal-binding / Multifunctional enzyme / Myristate / Nuclease / Nucleotidyltransferase / Nucleus / Phosphoprotein / RNA-binding / RNA-directed DNA polymerase / Transferase / Viral nucleoprotein / Virion / Zinc / Zinc-finger

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