Figure 5. The key allo-residues predicted by our method in Tar and PDZ3.

(A) The crystal structure of holo-Tar. Aspartate (Asp) is represented by magenta sticks, the allosteric pocket is represented by marine surface, and the salmon helix is selected as the orthosteric site. (B) The key allo-residues predicted at the Asp-binding site. The predicted key allo-residues in the allosteric cavity_2 are represented by marine sticks, among which Y149 and Q152 are the true key allo-residues that have been confirmed by experiments. Hydrogen bonds are shown as red dash lines. (C) The predicted key allo-residues in PDZ3. The peptide bound to the orthosteric site is represented by salmon sticks, the allosteric pocket is represented by marine surface, and the predicted key allo-residues are represented by marine sticks.