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. Author manuscript; available in PMC: 2019 Nov 19.
Published in final edited form as: J Med Chem. 2018 Dec 19;62(2):987–992. doi: 10.1021/acs.jmedchem.8b01723

Figure 2. Binding interactions of the inhibitor fatty acid to AC active site.

Figure 2.

(A) Close up view of the binding area in the complex (magenta and cyan ribbons for α– and β–subunits, respectively). The inhibitor moiety (yellow sticks) and the residues defining the interaction with the inhibitor (cyan sticks) are shown. The electron density map (grey) around the bound inhibitor is contoured at 1σ. Hydrogen bonds are indicated by grey dotted lines. (B) The part of the protein surface (in the same colors as in A) showing the deep channel into the active site with Cys143 covalently modified by the fatty acid (in yellow sticks) is presented.