Figure 6. Inhibitor Dap-Pip in the DPP7 active site.

(A) Omit and 2Fo-Fc electron density maps for the bound inhibitor are shown at 1 and 1.5σ, respectively. (B) General overview of the inhibitor in the binding pocket. The α/β–hydrolase domain is shown in aquamarine and the SKS–domain in green. The inhibitor is shown in magenta. (C) Stereo view of the residues involved in inhibitor binding. The coloring scheme is the same as above. Dashed yellow lines denote hydrogen bonding interactions (D) Representation of the interaction of the inhibitor with surrounding residues prepared using LigPlot+ [60]. (E) Superimposition of the DPP7 Dab-Pip complex with the structure of DPP4 complexed with Diprotin A [42]. The coloring scheme for DPP7 is the same as above. The Diprotin A is shown using thinner, yellow sticks. The figure was prepared using the program PyMOL (http://www.pymol.org/).