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TitleStructural and Kinetic Studies of Asp632 Mutants and Fully Reduced NADPH-Cytochrome P450 Oxidoreductase Define the Role of Asp632 Loop Dynamics in the Control of NADPH Binding and Hydride Transfer.
Journal, issue, pagesBiochemistry, Vol. 57, Page 945-962, Year 2018
Publish dateFeb 10, 2017 (structure data deposition date)
AuthorsXia, C. / Rwere, F. / Im, S. / Shen, A.L. / Waskell, L. / Kim, J.P.
External linksBiochemistry / PubMed:29308883
MethodsX-ray diffraction
Resolution1.9 - 2.7 Å
Structure data

PDB-5urd:
wild type rat CYPOR bound with NADP+ - oxidized form
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5ure:
Wild type rat CYPOR bound with NADP+ - reduced form
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5urg:
rat CYPOR D632F mutant
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5urh:
CYPOR/D632A with NADP+
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5uri:
Rat CYPOR/D632A with 2'-AMP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

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

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-2AM:
ADENOSINE-2'-MONOPHOSPHATE

Source
  • rattus norvegicus (Norway rat)
KeywordsOXIDOREDUCTASE / Flavoprotein / hydroquinone / reductase

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