3.8.1. RDF of PPARα complexes
The APHM13-PPAR complex included many hydrogen bonds but the Thr138: N was making the most consistent hydrogen bond interaction with the O35 atom of the ligand. Initially, the distribution peak was not sharp and exhibited the g(r) value of 0.61 at 3.01 Å whereas, at 100 ns, the sharp definite peak was observed having the g(r) value of 1.61 at 2.92 Å. After simulation, the highest distribution was observed at 4.9 Å with the g(r) value of 0.24. The peak was seen to be high in the middle of the simulation, and the density distribution expanded enhances the likelihood of the probability of finding ligand around Thr135. The lowering of density and increase in the distance occurred at the end simulation because of the involvement of the O35 atom of the ligand with another residue; Ala137.The active site residues of PPARα: Thr83 and Ser84 were found as vital residues involved in Hydrogen bond interaction with Forasartan (Radial Distribution Function calculated for (A) PPARα-APHM13, (B) PPARα-Forasartan, (C) PPARα-Lanifibranor, (D) PPARγ-Raltitrexed, (E) PPARγ-Lanifibranor, (F) PPARδ-Iloprost, (G) PPARδ-Lifitegrast, (H) PPARδ-Lanifibranor.The RDF of Gly66:N of PPARα and N9 atom of Lanifibranor was performed (