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Structure paper

TitleModulating Catalytic Activity by Unnatural Amino Acid Residues in a Gsh-Binding Loop of Gst P1-1.
Journal, issue, pagesJ. Mol. Biol., Vol. 376, Page 811-, Year 2008
Publish dateNov 8, 2006 (structure data deposition date)
AuthorsHegazy, U.M. / Tars, K. / Hellman, U. / Mannervik, B.
External linksJ. Mol. Biol. / PubMed:18177897
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-2j9h:
Crystal structure of human glutathione-S-transferase P1-1 cys-free mutant in complex with S-hexylglutathione at 2.4 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-GTX:
S-HEXYLGLUTATHIONE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / P1-1 / GLUTATHIONE / POLYMORPHISM / GLUTATHIONE TRANSFERASE

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