Overall views of Trametes versicolor GSTO3S structure in complex with glutathione and 2,4 hydroxy benzophenone (left panels) and GSTO6S structure in complex with naringenin (right panels). In each case, structures are depicted in cartoon mode with ligands shown as spheres and sticks (glutathione in green, 2,4-HBP and naringenin in yellow). N-terminal domains are shown in light colors (white for GSTO3S, cyan for GSTO6S) and C-terminal domains are shown in deeper colors (grey for GSTO3S, blue for GSTO6S). Black arrows indicate positions of glutathione binding site (G-site), hydrophobic binding site (H-site) and ligandin site (L-site). In each case is represented one physiological dimer that typifies the structure of GSTs where the N-terminal domain (secondary structure β1α1β2α2β3β4α3) of one monomer cross-interacts with the C-terminal domain (α4α5α6α6′α7α8α9) of the second one, and vice-versa.