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TitleCysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.
Journal, issue, pagesProteins, Vol. 71, Page 16-23, Year 2008
Publish dateMay 10, 2007 (structure data deposition date)
AuthorsAllocati, N. / Federici, L. / Masulli, M. / Favaloro, B. / Di Ilio, C.
External linksProteins / PubMed:18076047
MethodsX-ray diffraction
Resolution1.803 Å
Structure data

PDB-2pvq:
Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site
Method: X-RAY DIFFRACTION / Resolution: 1.803 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GSH:
GLUTATHIONE

ChemComp-HOH:
WATER

Source
  • ochrobactrum anthropi (bacteria)
KeywordsTRANSFERASE / xenobiotics detoxification / glutathione / H-site

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