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TitleAn intact eight-membered water chain in drosophilid alcohol dehydrogenases is essential for optimal enzyme activity.
Journal, issue, pagesFebs J., Vol. 279, Page 2940-2956, Year 2012
Publish dateApr 15, 2011 (structure data deposition date)
AuthorsWuxiuer, Y. / Morgunova, E. / Cols, N. / Popov, A. / Karshikoff, A. / Sylte, I. / Gonzalez-Duarte, R. / Ladenstein, R. / Winberg, J.O.
External linksFebs J. / PubMed:22741949
MethodsX-ray diffraction
Resolution1.45 - 1.98 Å
Structure data

PDB-3rj5:
Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-3rj9:
Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

Chemicals

ChemComp-ACY:
ACETIC ACID

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-HOH:
WATER

Source
  • scaptodrosophila lebanonensis (fry)
KeywordsOXIDOREDUCTASE / short-chain dehydrogenases/reductases / detoxification / NAD metabolism / short-chain dehydrogenase

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