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TitleHigh-Resolution Crystal Structure of Plant Carboxylesterase AeCXE1, from Actinidia eriantha, and Its Complex with a High-Affinity Inhibitor Paraoxon.
Journal, issue, pagesBiochemistry, Vol. 46, Page 1851-1859, Year 2007
Publish dateDec 11, 2006 (structure data deposition date)
AuthorsIleperuma, N.R. / Marshall, S.D. / Squire, C.J. / Baker, H.M. / Oakeshott, J.G. / Russell, R.J. / Plummer, K.M. / Newcomb, R.D. / Baker, E.N.
External linksBiochemistry / PubMed:17256879
MethodsX-ray diffraction
Resolution1.4 - 2.3 Å
Structure data

PDB-2o7r:
Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-2o7v:
Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-4PA:
PROPYL ACETATE

ChemComp-HOH:
WATER

ChemComp-DEP:
DIETHYL PHOSPHONATE

Source
  • actinidia eriantha (plant)
KeywordsHYDROLASE / carboxylesterase / Actinidia eriantha / alpha/beta hydrolase / AeCXE1 / paraoxon / insecticide

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