Footprinting of Inhibitor Interactions of In Silico Identified Inhibitors of Trypanothione Reductase of Leishmania Parasite
Figure 5
Binding Compound 31 (a) at the active site, the compound is lodged at the periphery of the active site, with potential hydrogen bonding interactions with Glu4666 and Glu467 making it a high-affinity interaction. Compound 47 (b) belonging to Cluster 4 binds to the additional hydrophobic patch with side chains extending towards the substrate-binding cleft.
