Footprinting of Inhibitor Interactions of In Silico Identified Inhibitors of Trypanothione Reductase of Leishmania Parasite
Figure 2
Orientation of inhibitors segregated into four different clusters at the active site of TR. Inhibitors in Cluster 1 (a) position themselves between both the hydrophobic patches of the active site, Cluster 2 (b) bind to the Z site with their side chains orienting themselves towards the negatively charged residues of the active site. In Cluster 3 (c), the ligands primarily bind to the negatively charged residues such as Glu466, Glu467 residues involved in orientation of active site histidine during hydride transfer process, in Cluster 4 (d) comprise of compounds which stack to the Z site, in the vicinity of the active site and they also interact with Lys61 of the substrate-binding site.
