Fig. 3: BiteNet predictions for the energy minimization trajectory of the assymetric dimer structure of the EGFR kinase domain.
From: Spatiotemporal identification of druggable binding sites using deep learning
a Assymetric dimer structure of the EGFR kinase domain. Orthosteric and allosteric ligands are shown with yellow and magenta sticks, respectively, Mg ion is shown as green sphere. b BiteNet predictions for the assymetric dimer, the predicted centers for the ligands are shown as spheres with the corresponding color. c BiteNet predictions obtained for the energy minimization trajectory. The normalized energy is shown with blue dash-dotted line, the RMSD with respect to the unbound conformation of the alloteric binding site is shown with violet dotted line, BiteNet probability score for the orthosteric and allosteric binding sites are shown with dashed orange and magenta solid lines, respectively. The normalized energy of 1 and 0 corresponds to  −7.76969 × 105 kJ/mol and  −8.80655 × 105 kJ/mol, respectively. d The starting and the final conformations of the minimization trajectory along with BiteNet predictions.
