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TitleStructural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action.
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 12860-12867, Year 2004
Publish dateDec 23, 2003 (structure data deposition date)
AuthorsVan Den Heuvel, R.H. / Westphal, A.H. / Heck, A.J. / Walsh, M.A. / Rovida, S. / Van Berkel, W.J. / Mattevi, A.
External linksJ. Biol. Chem. / PubMed:14703520
MethodsX-ray diffraction
Resolution2.1 - 2.2 Å
Structure data

PDB-1rz0:
Flavin reductase PheA2 in native state
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1rz1:
Reduced flavin reductase PheA2 in complex with NAD
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

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

Source
  • geobacillus thermoglucosidasius (bacteria)
KeywordsOXIDOREDUCTASE / flavin / FAD / NAD

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