Later, molecular docking simulations were performed using HDOCK software, and the resulting CD19-TYRP and CD28-TYRP complexes are shown in Figure . The proteins lock one another for appropriate binding in both scenarios. Visual inspection of the receptor complexes further confirms that the interactions were governed by charge complementarity, as shown in Figure . Furthermore, we have discovered that the binding occurs at the protein's druggable region, which is predicted by the graph neural network. We think that significant conformational changes are necessary for the receptors to interact because the druggable sites of the protein are located in the lower part of the protein. We assume that the amino acids at the protein's druggable region and the electrostatic surface charge cause these interactions. In addition, we have also computed the number of interactions (hydrogen bonds) formed between the receptors using an in-house script. Based on our script, the CD19-TYRP complex formed 54, and the CD28-TYRP complex framed 41 hydrogen bonds.