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TitleOrigin of the Proton-Transfer Step in the Cofactor-Free 1-H-3-Hydroxy-4-Oxoquinaldine 2,4- Dioxygenase: Effect of the Basicity of an Active Site His Residue.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 8620-, Year 2014
Publish dateNov 19, 2013 (structure data deposition date)
AuthorsHernandez-Ortega, A. / Quesne, M.G. / Bui, S. / Heuts, D.P. / Steiner, R.A. / Heyes, D.J. / De Visser, S.P. / Scrutton, N.S.
External linksJ. Biol. Chem. / PubMed:24482238
MethodsX-ray diffraction
Resolution1.94 Å
Structure data

PDB-4cfs:
CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HQD:
3-HYDROXY-2-METHYLQUINOLIN-4(1H)-ONE

ChemComp-TAR:
D(-)-TARTARIC ACID

ChemComp-HOH:
WATER

Source
  • arthrobacter nitroguajacolicus (bacteria)
KeywordsOXIDOREDUCTASE / ALPHA-BETA HYDROLASE COMPLEX / DIOXYGENASE / COFACTOR-DEVOID

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