Footprinting of Inhibitor Interactions of In Silico Identified Inhibitors of Trypanothione Reductase of Leishmania Parasite
Figure 3
Compound 16 (a) of cluster 1 traversed between hydrophobic patches formed by Trp21, Met114 and Leu399, Pro492, and Pro398 where later is located in vicinity to the substrate-binding site, it also showed hydrogen bonding potential with Tyr110 of the active site, Tyr110 anchors the substrate to the active site by hydrogen bonding with the spermidine moiety. Compound 48 (b) of Cluster 2 binds to the Z site with hydrogen bonding potentials with His461, active site histidine base, and also with the residues which aid in orientation of substrate towards the active site.
