Considering that proteins are functional molecules of living cells, having knowledge of how they function can be effective. Among the important and effective factors in the function of proteins is their three-dimensional structure. Glutathione S-transferase enzyme is one of the proteins present in living cells that participates in the transformation and detoxification of xenobiotic compounds. In this study, the 3-dimensional structure of the Glutathione S-transferase protein isolated from Shigella dysanteriae, which has not been determined experimentally, was simulated by aligning with E. coli (strain K12) sequences with the Swiss model program. The alignment result showed that the GST gene has 84% ​​similarity compared to the human gene. The results also showed that leucine was the constituent amino acid of this protein, which accounted for a greater amount of the protein composition than other amino acids. In order to examine the quality of modeling, Root Mean Square (RMS) was calculated, which was 0.47 angstroms in the model in question, which was less than 1, indicating the suitability of the designed model. By determining and predicting the structure and modeling of enzymes, it is possible to study the interactions between residues and their substrates and effectively use bioinformatics modeling methods in the field of drug and vaccine manufacturing.