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. 2019 Dec 11;4(26):22161–22168. doi: 10.1021/acsomega.9b03409

Figure 2.

Figure 2

Docking studies of compound 7 with AChE and MAO-B. (A) Proposed docked pose of 7 in the active site of AChE (PDB-ID: 1B41). Compound 7 is rendered with cyan sticks. The side-chain conformations of active site amino acids are shown, including the mobile residues of Trp86, Tyr72, Asp74, Tyr124, Trp286, Tyr337, and Tyr341. The catalytic triad is colored in green, the oxyanion hole in magenta, the CAS and the acyl-binding pocket in orange, and the PAS in light blue. (B) Binding mode prediction of compound 7 in the active site of MAO-B (PDB-ID: 2V5Z). Compound 7 is rendered with yellow sticks. The amino acid residues that are involved in inhibitor binding are shown. The FAD cofactor and the six water molecules as an integral part of the MAO-B structure model are displayed as orange sticks and light red balls, respectively. Intermolecular interactions are shown as dashed lines according to their type: green, hydrogen bond; blue, hydrogen bond to water; purple, π–π T-shaped interaction; pink, π–alkyl and alkyl–alkyl contacts.