RESUMEN
Glutathione S-transferases (GST) belong to the transferase group of enzymes; GST are a family of enzymes that catalyze the addition of glutathione to endogenous or xenobiotic, often toxic electrophilic chemicals, and a major group of detoxification enzymes. We used the homology modeling technique to construct the structure of Gallus gallus GST. The amino acid sequence identity between the target protein and sequence of template protein 1ML6 (Mus musculus) was 66.2%. Based on the template structure, the protein model was constructed by using the Homology program Modeller9v1, and briefly refined by energy minimization steps; it was validated by PROCHECK. In all, 94.4% of the amino acids were in allowed regions of Ramachandran plot, showing the accuracy of the model and good stereochemical quality. Our results correlated well with the experimental data reported earlier, which proved the quality of the model. This generated model can be further used for the design and development of more potent GST inhibitors.