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Structure paper

TitleThe multi-functional role of a highly conserved aspartic acid residue in glutathione transferase P1-1
Journal, issue, pagesTo be Published
Publish dateJul 2, 2003 (structure data deposition date)
AuthorsKong, G.K.-W. / Polekhina, G. / McKinstry, W.J. / Parker, M.W. / Dragani, B. / Aceto, A. / Paludi, D. / Principe, D.R. / Mannervik, B. / Stenberg, G.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.03 - 2.1 Å
Structure data

PDB-1px6:
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1px7:
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

Chemicals

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-GSH:
GLUTATHIONE

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / glutathione transferase / helix capping / mutations / protein folding

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