3l0h | pdb_00003l0h

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Template:STRUCTURE 3l0h

Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione

Template:ABSTRACT PUBMED 20833278

Function

[GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[1]

About this Structure

3l0h is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  1. Balchin D, Fanucchi S, Achilonu I, Adamson RJ, Burke J, Fernandes M, Gildenhuys S, Dirr HW. Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1. Biochim Biophys Acta. 2010 Sep 15. PMID:20833278 doi:10.1016/j.bbapap.2010.09.003
  1. ↑ Achilonu I, Gildenhuys S, Fisher L, Burke J, Fanucchi S, Sewell BT, Fernandes M, Dirr HW. The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jul 1;66(Pt, 7):776-80. Epub 2010 Jun 23. PMID:20606271 doi:10.1107/S1744309110019135

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