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Structure paper

TitleStructural, kinetic, and thermodynamic studies of specificity designed HIV-1 protease.
Journal, issue, pagesProtein Sci., Vol. 21, Page 1029-1041, Year 2012
Publish dateApr 16, 2012 (structure data deposition date)
AuthorsAlvizo, O. / Mittal, S. / Mayo, S.L. / Schiffer, C.A.
External linksProtein Sci. / PubMed:22549928
MethodsX-ray diffraction
Resolution1.69 - 1.9 Å
Structure data

PDB-4ep2:
Crystal Structure of inactive single chain wild-type HIV-1 Protease in Complex with the substrate RT-RH
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4ep3:
Crystal Structure of inactive single chain wild-type HIV-1 Protease in Complex with the substrate CA-p2
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-4epj:
Crystal Structure of inactive single chain wild-type HIV-1 Protease in Complex with the substrate p2-NC
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

PDB-4eq0:
Crystal Structure of inactive single chain variant of HIV-1 Protease in Complex with the substrate p2-NC
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4eqj:
Crystal Structure of inactive single chain variant of HIV-1 Protease in Complex with the substrate RT-RH
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-ACT:
ACETATE ION

Source
  • hiv-1 m:b_arv2/sf2 (virus)
  • human immunodeficiency virus 1
Keywordshydrolase/hydrolase substrate / HIV-1 protease / specificity design / drug design / Protease inhibitors / AIDS / Aspartyl protease / HYDROLASE / hydrolase-hydrolase substrate complex

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