Figure 3.

On the left, the best docking conformation of lamellarin D (AR010 in stick) inside the enzymatic binding site. The binding site is represented as a solvent accessible surface (SAS) colored according to the hydrophobicity of the residues (wireframe). The two key residues of the catalytic dyad (H⁴¹ and C¹⁴⁵) are rendered in CPK, and the four binding pockets (S1^I, S1, S2, and S4) occupied by the molecule are highlighted. On the right, a two-dimensional representation of the molecular interactions between the ligand and the enzyme. The colors used refer to the different interactions, as indicated in the legend.