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The 3D structure of the Z-glutathione transferase was obtained from the Protein Data Bank (PDF) under the code 1FW1, this protein has a sequence of 208 residue (5to 212). The model obtained consists of 208 amino acids, 1 sulfate ion, a molecule of glutathione, a molecule of 2,3-dihydroxy-1, 4-ditiobuano (DTT) and 109 water molecules. Being the residue Ser10; responsible for the catalytic activity. Despite some differences in numerical values of the functions of evaluation and taking into account the error associated with the use of methods derived from classical mechanics the results of molecular docking were quite adequate to estimate the possible location and conformation of adducts formed between glutathione and acid-α Haloalkane, these results showed a good agreement between geometric found to α-Haloalkane and the active site, this compouns did not show significant differences regarding stereoselectivity and stereospecificity of GSTZ towards acids α-Haloalkane. Additionally, the results suggest that the ligands studied have enough mobility within the active site to generate poses with high affinity binding but with little probability of occurrence, which may be due to the orientation they assume some hydrogen atoms.
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