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TitleStructural Basis of the Suppressed Catalytic Activity of Wild-Type Human Glutathione Transferase T1-1 Compared to its W234R Mutant.
Journal, issue, pagesJ. Mol. Biol., Vol. 355, Page 96-, Year 2006
Publish dateOct 11, 2005 (structure data deposition date)
AuthorsTars, K. / Larsson, A.-K. / Shokeer, A. / Olin, B. / Mannervik, B. / Kleywegt, G.J.
External linksJ. Mol. Biol. / PubMed:16298388
MethodsX-ray diffraction
Resolution1.5 - 2.4 Å
Structure data

PDB-2c3n:
Human glutathione-S-transferase T1-1, apo form
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2c3q:
Human glutathione-S-transferase T1-1 W234R mutant, complex with S- hexylglutathione
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2c3t:
Human glutathione-S-transferase T1-1, W234R mutant, apo form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

ChemComp-GTX:
S-HEXYLGLUTATHIONE

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / GLUTATHIONE / GLUTATHIONE TRANSFERASE / T1-1 / POLYMORPHISM

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