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. Author manuscript; available in PMC: 2011 Dec 16.
Published in final edited form as: J Phys Chem B. 2010 Oct 11;114(49):16263–16272. doi: 10.1021/jp108056s

Figure 9.

Figure 9

Snapshots of the binding site of each ternary complex depicting the ligand, phosphate, and important interactions with neighboring residues taken from the simulated structures averaged over the last 500 ps of MD simulations. Plots of the average distance between the inhibitor atom and a heavy atom of the protein residues within hydrogen bonding distance for each chain of the complexes. The 2′-OH is absent from DAT and H7 is absent on INO, these distances are set as zero value. Interactions are best maintained in the late TS inhibitors DAT and DAD. A chemical representation of the binding site shows the interactions of INO with neighboring residues represented in the distance plots. Interaction between Thr242 and the inhibitors is shown in the distance plots, but is absent in the snapshots of the active site for clarity.