In this study, all-atom unrestrained μs long MD simulations of the GluK1 protein receptor in an aqueous solution were performed to explore the glutamate binding mechanism to the receptor. Experimental studies suggest that protein undergoes significant conformational chances and has a unique glutamate binding mechanism discussed in this section using molecular dynamics simulations. Furthermore, inhibitors against this receptor have also been proposed using molecular docking simulations. The computed root-mean-square deviation (RMSD) values of Cα atoms indicated that the relaxation of these structures requires at least 200ns of simulation time.