In the present study, molecular docking and molecular dynamics techniques were employed to investigate the functionality of the Kainate Receptor (GluK1) and to predict potential inhibitors targeting this receptor. We hypothesized that the glutamate binding and unbinding in the receptor cavity should result in major conformational changes (cavity opening and closing activity) in the glutamate binding site. In addition, in the absence of the glutamate, the GluK1 receptor cavity should shrink and expand in the presence of it. Our research unveiled the dynamic behavior of the protein, particularly its interactions with glutamate, in comparison to its interactions with pharmaceutical compounds. The identification of inhibitors for GluK1-1a Kainate receptor and subsequent structural analysis thereof would contribute significantly to advancing our comprehension, thereby facilitating the development of pharmaceutical agents capable of modulating the Kainate receptor and subsequently influencing the associated neural pathways, either propagating or inhibiting them as a consequential outcome.