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Structure paper

TitleRole of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 42188-42197, Year 2005
Publish dateJul 30, 2005 (structure data deposition date)
AuthorsZhao, B. / Guengerich, F.P. / Voehler, M. / Waterman, M.R.
External linksJ. Biol. Chem. / PubMed:16239228
MethodsX-ray diffraction
Resolution1.8 - 2.15 Å
Structure data

PDB-2d09:
A Role for Active Site Water Molecules and Hydroxyl Groups of Substrate for Oxygen Activation in Cytochrome P450 158A2
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2d0e:
Substrate assited in Oxygen Activation in Cytochrome P450 158A2
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-FLV:
FLAVIOLIN

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-HOH:
WATER

ChemComp-NQ:
2-HYDROXYNAPHTHOQUINONE

Source
  • streptomyces coelicolor (bacteria)
KeywordsOXIDOREDUCTASE / streptomyces / Cytochrome P450 oxidoreductase / CYP158A2 / proton transfer / dioxygen activation / 2-hydroxy-1 / 4-naphthoquinone

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