3-hydroxy-3-methylglutaryl CoA reductase is considered as an essential enzyme due to its inevitability in the Mevalonate pathway for the synthesis of isoprenoids in plants. In this study, theoretical investigations were accomplished for comparative protein model and active site analyses of Triticum aestivum HMG-CoA reductase (designated as TaHMGR) as there are no three-dimensional structures available for this species in Protein Data Bank. So, to fulfill the necessity of this structure we built

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... the comparative protein model, evaluated using different criteria and finally deposited in Protein Model Database (PMDB). We used different Bioinformatics tools and servers to carry out this research. The selected enzyme contains disordered regions and the residues Glycine, Serine, Lysine, and Proline are mainly responsible for these regions as found by our research. We also found 3 ligand binding sites with the high quantity of Glycine, Valine, and Alanine residues in their binding sites and the significant Z-score ensures these findings. The biochemical function was found as a catalytic and binding activity with the significance score, which confirms the actual function of TaHMGR. The attained data convey necessary fundamental information about this enzyme to pave the way in improving the structure-based drug development using T. aestivum species.