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TitleCrystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per subunit
Journal, issue, pagesTo be Published
Publish dateJan 22, 2013 (structure data deposition date)
AuthorsVetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. ...Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / Hillerich, B. / Love, J. / Seidel, R.D. / Imker, H.J. / Armstrong, R.N. / Gerlt, J.A. / Almo, S.C. / Enzyme Function Initiative (EFI)
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-4ivf:
Crystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per subunit
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-GSH:
GLUTATHIONE

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

Source
  • lodderomyces elongisporus (fungus)
KeywordsTRANSFERASE / GST / glutathione S-transferase / Enzyme Function Initiative / EFI / Structural Genomics

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