To perform dynamic scanning "Dy-FMOPhore", supervised molecular dynamics (SuMD) is used to create a whole ensemble sampling phase between the target binding site and probes (in case of apo-scenario) or ligands (in case of holo-scenario), independent from the initial ligand position either in solvent or within the binding site vicinity. Protein structures, are prepared with the protein preparation wizard as implemented in Maestro. Hydrogen atoms are added to the complex and missing atoms in protein side chains were built according to the AMBER16 force field topology. With the Dy-FMOPhore it is possible to assess binding interaction throughout a full MD simulation trajectory. First, we used FMOPhore to analyse multiple co-crystalized holo-complexes for each system, using FP-score to classify the binding site residues (Hotspots and Non-hotspots)