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Structure paper

TitleStructural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases.
Journal, issue, pagesJ. Mol. Biol., Vol. 420, Page 190-203, Year 2012
Publish dateDec 16, 2010 (structure data deposition date)
AuthorsZhou, H. / Brock, J. / Liu, D. / Board, P.G. / Oakley, A.J.
External linksJ. Mol. Biol. / PubMed:22522127
MethodsX-ray diffraction
Resolution1.7 - 2 Å
Structure data

PDB-3q18:
Human Glutathione Transferase O2
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3q19:
Human Glutathione Transferase O2
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3qag:
Human Glutathione Transferase O2 with glutathione -new crystal form
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3vln:
Human Glutathione Transferase O1-1 C32S Mutant in Complex with Ascorbic Acid
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GSH:
GLUTATHIONE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SO4:
SULFATE ION

ChemComp-ASC:
ASCORBIC ACID / medication*YM

ChemComp-ACT:
ACETATE ION

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Glutathione Transferase / GST / Dehydroascorbate Reductase / Reductase / GST fold / glutathione

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