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TitleTwo alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.
Journal, issue, pagesProteins, Vol. 66, Page 219-228, Year 2007
Publish dateAug 9, 2016 (structure data deposition date)
AuthorsDeemagarn, T. / Wiseman, B. / Carpena, X. / Ivancich, A. / Fita, I. / Loewen, P.C.
External linksPubMed:17063492
MethodsX-ray diffraction
Resolution1.8 - 2.15 Å
Structure data

PDB-5sx1:
Crystal structure of D141E variant of B. pseudomallei KatG
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5sx2:
Crystal structure of the D141E mutant of B. pseudomallei KatG at pH 8.0.
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-NA:
Unknown entry

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • burkholderia pseudomallei (strain 1710b) (bacteria)
KeywordsOXIDOREDUCTASE / KatG / catalase-peroxidase

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