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Structure paper

TitleDifferent binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.
Journal, issue, pagesBiochemistry, Vol. 46, Page 8725-8733, Year 2007
Publish dateApr 12, 2006 (structure data deposition date)
AuthorsZhao, B. / Lamb, D.C. / Lei, L. / Kelly, S.L. / Yuan, H. / Hachey, D.L. / Waterman, M.R.
External linksBiochemistry / PubMed:17614370
MethodsX-ray diffraction
Resolution1.97 - 2.9 Å
Structure data

PDB-2dkk:
Structure/Function studies of Cytochrome P450 158A1 from Streptomyces Coelicolor A3(2)
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-2nz5:
Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2)
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-2nza:
Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2)
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-IMD:
IMIDAZOLE

ChemComp-HOH:
WATER

ChemComp-226:
naphthalene-1,2,4,5,7-pentol

Source
  • streptomyces coelicolor (bacteria)
KeywordsOXIDOREDUCTASE / streptomyces / Cytochrome P450 oxidoreductase / CYP158A1 / inhibitor / streptomyces; Cytochrome P450 oxidoreductase; CYP158A1; flaviolin; C-C coupling activity

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