Published Paper Details:

Tuberculosis, caused by Mycobacterium Tuberculosis (Mtb), is a leading cause of death, with 10.7 million new cases and 1.23 million deaths expected worldwide by 2024. The Hypoxanthine guanine phosphoribosyltransferase protein (hpt) belongs to the purine/pyrimidine phosphoribosyl transferase (PRTase) family and is used to discover active ligand molecules that inhibit the purine salvage pathway. The homology simulated 3D model was created with modeler 9.13 software. The final structure was validated, and the active site was identified using pre-requisite predictitions. The protein's three-dimensional structure consists of nine sheets and twelve helices. The grid was built on the active site, followed by virtual screening using the drug bank ligand database. The majority of the lead compounds acquired contain imidazole moieties and derivatives as pharmacophore groups in their structures. The target protein amino acid residues identified by virtual screening are Val69, Asp74, Arg77, Ile79, and Pro80, which are critical for ligand binding. The chosen lead compounds have permitted ADME characteristics and can inhibit the purine salvage pathway in Mtb. The imidazole structural scaffolds can be found in the ligand molecules of docked complexes Lig1, Lig 2, and Lig 3.