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Structure paper

TitleStructural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
Journal, issue, pagesFEBS J., Vol. 284, Page 2442-2463, Year 2017
Publish dateNov 24, 2015 (structure data deposition date)
AuthorsPegeot, H. / Mathiot, S. / Perrot, T. / Gense, F. / Hecker, A. / Didierjean, C. / Rouhier, N.
External linksFEBS J. / PubMed:28622459
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-5ey6:
CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE F2 FROM POPULUS TRICHOCARPA
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5f05:
Crystal structure of glutathione transferase F5 from Populus trichocarpa
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5f06:
Crystal structure of glutathione transferase F7 from Populus trichocarpa
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5f07:
Crystal structure of glutathione transferase F8 from Populus trichocarpa
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GSH:
GLUTATHIONE

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

ChemComp-12P:
DODECAETHYLENE GLYCOL / precipitant*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-SO4:
SULFATE ION

Source
  • populus trichocarpa (black cottonwood)
KeywordsTRANSFERASE / glutathione / ligandin

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