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. Author manuscript; available in PMC: 2018 May 16.
Published in final edited form as: Org Biomol Chem. 2017 May 16;15(19):4096–4114. doi: 10.1039/c7ob00526a

Fig. 3.

Fig. 3

Upon inhibitor binding, the loops containing the Thr 509-Thr 613 pair collapse to form an amphiphilic binding site at the indole 5-position. (a) Polar subsite: the Thr γ-hydroxyls engage in a network of hydrogen bonds with polar inhibitor substituents. (b) Hydrophobic subsite: rotation of the Thr χ1 torsions by 150–180° results in γmethyl group interactions with small hydrophobic moieties on the indole 5-position. In this conformation, the bridging water molecule has been displaced from the binding pocket.