Fig. 4 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 4. Docking of compounds 3, 9, 11, and 15 in human lipase enzyme. The original structure of the lipase enzyme (1LPB) contains the inhibitor methoxyundecylphosphinic acid (MUP, carbons coloured purple (A)). The docking results in lipase enzyme (B-E, green surface) with compounds 3 (pink, B), 9 (cyan, C), 11 (magenta, D), and 15 (green, E) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (S169, D193, and H280). Residues making hydrogen bonds with the ligands are indicated (B–E). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)