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TitleStructures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 97, Page 3177-3182, Year 2000
Publish dateOct 1, 1999 (structure data deposition date)
AuthorsFaig, M. / Bianchet, M.A. / Talalay, P. / Chen, S. / Winski, S. / Ross, D. / Amzel, L.M.
External linksProc. Natl. Acad. Sci. USA / PubMed:10706635
MethodsX-ray diffraction
Resolution1.7 - 2.8 Å
Structure data

PDB-1d4a:
CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1dxo:
Crystal structure of human NAD[P]H-QUINONE oxidoreductase CO with 2,3,5,6,tetramethyl-P-benzoquinone (duroquinone) at 2.5 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1dxq:
CRYSTAL STRUCTURE OF MOUSE NAD[P]H-QUINONE OXIDOREDUCTASE
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-DQN:
DUROQUINONE

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsOXIDOREDUCTASE / FLAVOPROTEIN / ROSSMANN FOLD / DT-DIAPHORASE / CANCER / CHEMOPROTECTION / CHEMOTHERAPY / DEHYDROGENASEROSSMAN FOLD

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