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Structure paper

TitleThe enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 275, Page 3296-3304, Year 2000
Publish dateMay 26, 1998 (structure data deposition date)
AuthorsPatskovsky, Y.V. / Patskovska, L.N. / Listowsky, I.
External linksJ. Biol. Chem. / PubMed:10652317
MethodsX-ray diffraction
Resolution2.55 Å
Structure data

PDB-2gtu:
LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / GLUTATHIONE / CONJUGATION / DETOXIFICATION / CYTOSOLIC / DIMER

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