Figure 3 | Scientific Reports

Figure 3

From: New 2-Aryl-9-methyl-β-carbolinium salts as Potential Acetylcholinesterase Inhibitor agents: Synthesis, Bioactivity and Structure–Activity Relationship

Figure 3

The estimated binding modes of the compounds into the active site of AChE and BuChE. The protein structures are show in Ribbon style with coil in green, helix in red and strand in yellow. The binding site residues are displayed using a stick model with carbon in green. The potential hydrogen contacts between compounds and protein were highlighted by yellow dashed lines. (A) Superposition of huprine W in the X-ray crystallographic structure (PDB code 4BDT; orange) and in docking resultant complex structure of the AChE (dark green). (B–E) The binding modes of the compounds (in stick model with carbon) into the active site of AChE: (B) B22 (cyan) and A22 (pink); (C) B22 (cyan) and B21 (goldenrod); (D) B19 (chartreuse) and B18 (medium blue); (E) B16 (purple) and B15 (orange red). (F) The binding modes of compounds B22 (cyan) and A22 (pink) into the active site of BuChE. Other atoms were colored as follows: nitrogen, blue; oxygen, red; hydrogen, gray.

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