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Structure paper

TitleStructures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.
Journal, issue, pagesJ. Mol. Biol., Vol. 295, Page 357-374, Year 2000
Publish dateNov 29, 1999 (structure data deposition date)
AuthorsCunane, L.M. / Chen, Z.W. / Shamala, N. / Mathews, F.S. / Cronin, C.N. / McIntire, W.S.
External linksJ. Mol. Biol. / PubMed:10623531
MethodsX-ray diffraction
Resolution2.5 - 2.75 Å
Structure data

PDB-1dii:
CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1diq:
CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-CL:
Unknown entry

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

ChemComp-HEC:
HEME C

ChemComp-HOH:
WATER

ChemComp-PCR:
P-CRESOL

Source
  • pseudomonas putida (bacteria)
KeywordsOXIDOREDUCTASE / FLAVOCYTOCHROME / ELECTRON-TRANSFER / FAD / HEME / P-CRESOL

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