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Structure paper

TitleContribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 585, Page 25-31, Year 2015
Publish dateJul 15, 2015 (structure data deposition date)
AuthorsRobinson, R. / Qureshi, I.A. / Klancher, C.A. / Rodriguez, P.J. / Tanner, J.J. / Sobrado, P.
External linksArch. Biochem. Biophys. / PubMed:26375201
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-5cku:
Structure of Aspergillus fumigatus ornithine hydroxylase (SidA) mutant N323A bound to NADP and ornithine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

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

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-ORN:
L-ornithine

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • neosartorya fumigata (strain atcc mya-4609 / af293 / cbs 101355 / fgsc a1100) (mold)
KeywordsOXIDOREDUCTASE / SIDEROPHORE / FLAVIN

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