To grow the scaffold fragment to the Indeglitazar, they maintain binding interaction with key Hotspot residues, and achieved strong hydrophobic and hydrogen bond interactions with key residues, Tyr-A-327, Arg-A-288, and Ser-A-289, forming pocket B, which were labeled as Anchor and Transient-category residues as per categories in the FP-score plot. This demonstrated pan-agonist activity profile in cells (EC50 (μM): 0.85) as well as biochemically (EC50s (μM):0.37). Accordingly, increase reaching to these key critical interactions mentioned by the FMOPhore-apo scan is predicted to increase potency. An analysis of interaction bond types and the 3D-spatial arrangement of functional groups, of both molecules compared to the 3D-FMOPhore model derived from the apostructure, suggests that FMOPhore is capable of reliably generating an optimal pharmacophore model at the binding site, even in the absence of prior knowledge of bound ligands, (Figure .). The carboxylic moiety on both the fragment and the leadcompound is typically aligned to the hydrogen bond acceptor, Pi-Pi stacking, and the hydrophobic features of the 3D-FMOPhore model (generated from the apo-structure scanning).