3.7.1. Hydrogen bond analysis of PPARα complexes
Tyr138
In APHM13-PPARα several residues were participating in hydrogen bonds and contributing to the stability. The residues of PPARα Asn23, Met24, Thr83, Thr87, Ala137, and Thr138 were involved in making hydrogen bonding with APHM13. All these residues were making more than one hydrogen bond except Thr83. Asn23, Met24, and Thr87 formed hydrogen bonds with O2 and O4 of the ligand. These bonds were forming and interchanging with one another during the simulation. Asn23 and Met24 were not seen forming bonds after 160 ns and 150 ns respectively while can also be seen forming hydrogen bonds at 200ns with O2 of the APHM13. The OH of Tyr138 was forming the hydrogen bond with O2 and O4, and O35 of the ligand was interacting with N of Tyr138. Tyr138 with O35 was making a strong and consistent bond till 180 ns after that the bond was not observed in the plot. Forasartan interacting with PPARα formed two hydrogen bonds (Hydrogen bond analysis of (A) PPARα-Forasartan, (B) PPARα-Lanifibranor, (C) PPARγ-Raltitrexed, (D) PPARγ-Lanifibranor, (E) PPARδ-Lifitegrast, (F)PPARδ-Lanifibranor.