In the next step, molecular docking simulations were performed on the protein to obtain ligands/inhibitors binding strongly to the protein. The molecular docking results further validated the predicted druggable site as all the ligands binds to this site. Based on our docking simulations five ligands (Ligand I, II, III, IV, and V) were selected for further analysis. The OAT1-ligands interactions are shown in Figure . In this figure the ligands are shown in blue while OAT1 amino acids are shown in pink as shown in Figure .The docking simulations were performed using Autodock simulations and Protein Ligand Interaction Profiler (PLIP) web server was used to predict the interactions between the OAT1 and ligand. Based on our analysis Ligand I formed three hydrophobic interactions with Ile226, Phe438, and Phe442 at a distance of 3.97, 3.59, and 3.65 Å, respectively. In addition, it forms one hydrogen bond with shows that all the compounds show high drug likeness. Interestingly, Ligand II, III, and IV are isomers and further evaluation of these protein-ligand complexes is required by using molecular dynamics simulations.