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Structure paper

TitleAn oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.
Journal, issue, pagesNature, Vol. 539, Page 593-597, Year 2016
Publish dateSep 6, 2016 (structure data deposition date)
AuthorsOrtmayer, M. / Lafite, P. / Menon, B.R. / Tralau, T. / Fisher, K. / Denkhaus, L. / Scrutton, N.S. / Rigby, S.E. / Munro, A.W. / Hay, S. / Leys, D.
External linksNature / PubMed:27851736
MethodsX-ray diffraction
Resolution1.65 - 1.9 Å
Structure data

PDB-5lte:
Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-5lth:
Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM) in complex with the dimethylamine substrate
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

PDB-5lti:
Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM) in complex with the dimethylamine substrate
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-ETX:
2-ETHOXYETHANOL

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-DMN:
DIMETHYLAMINE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-NO:
NITRIC OXIDE

Source
  • pseudomonas mendocina (strain ymp) (bacteria)
  • pseudomonas mendocina (bacteria)
KeywordsOXIDOREDUCTASE / heme binding / PAS domain / amine oxidase / dimethylamine

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