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. 2008 Nov 21;283(47):32880–32888. doi: 10.1074/jbc.M805484200

FIGURE 1.

FIGURE 1.

Dimeric structure (side view) of human GST π (PDB 9GSS) crystallized with S-hexylglutathione, which is colored green. This structure shows the electrostatic region between two subunits. Each individual subunit is colored-coded: the backbone of subunit A is shown in cyan, while that of subunit B is red. The residues selected for mutagenesis at the subunit interface are Arg-70, Arg-74, Asp-90, Asp-94, and Thr-67. The side chains of the A subunit amino acid residues are in yellow, whereas those of the B subunit are purple.