Figure 4: Decomposition of the binding free energy for the residues in the binding sites of PLY.
From: Insights into structure and activity of natural compound inhibitors of pneumolysin
Based on the MM-GBSA method performed for PLY-inhibitor complex systems, Leu460 and Tyr461 have appreciable Van der Waals (ΔEvdw) contributions, and Val372 also has a strong Van der Waals interaction of ≤−2.0 kcal/mol with CHO (A), CAM (B), SIO (C), BRA (D) and SIG (E).
