Figures & data
Figure 2. Axillaridine–A located at the aromatic gorge of AChE (PDB code: 1B41) after 2-ns MD simulation. Only the active site amino acids are labeled for the sake of clarity.
![Figure 2. Axillaridine–A located at the aromatic gorge of AChE (PDB code: 1B41) after 2-ns MD simulation. Only the active site amino acids are labeled for the sake of clarity.](/cms/asset/fab18d2f-6e7a-4d88-bcab-535aeeb19719/ienz_a_363448_f0002_b.gif)
Figure 3. Important amino acid residues within 5.0 å at the active site of AChE after 2-ns MD simulation. For detail refer to the text.
![Figure 3. Important amino acid residues within 5.0 å at the active site of AChE after 2-ns MD simulation. For detail refer to the text.](/cms/asset/088515af-2113-479f-a9e2-806fb652838f/ienz_a_363448_f0003_b.gif)
Figure 4. Size (Å) of the aromatic gorge between Glu81/Try286 (Upper) and Phe338/Trp86 (Lower) during 2-ns AChE-Axillaridine-A simulation.
![Figure 4. Size (Å) of the aromatic gorge between Glu81/Try286 (Upper) and Phe338/Trp86 (Lower) during 2-ns AChE-Axillaridine-A simulation.](/cms/asset/c44ee4d1-f19d-4ec1-b394-48e06faf345b/ienz_a_363448_f0004_b.gif)
Figure 5. Stable π–π interactions between Trp286/Tyr72 (Lower) and the aromatic ring of Axillaridine–A/Tyr124 (Upper) as a function of time in the AChE-Axillaridine-A simulation.
![Figure 5. Stable π–π interactions between Trp286/Tyr72 (Lower) and the aromatic ring of Axillaridine–A/Tyr124 (Upper) as a function of time in the AChE-Axillaridine-A simulation.](/cms/asset/3c10e361-5796-4ff7-80f9-753385eaa735/ienz_a_363448_f0005_b.gif)
Figure 6. π-π Interaction between the aromatic ring of Axillaridine-A (shown in gray color) and that of the Tyr124 residue (shown in orange color).
![Figure 6. π-π Interaction between the aromatic ring of Axillaridine-A (shown in gray color) and that of the Tyr124 residue (shown in orange color).](/cms/asset/6a225728-41e2-495d-85b8-7bf8e6a1389f/ienz_a_363448_f0006_b.gif)
Table 1. Summary of the average distances between heavy atoms (Å) for important stable hydrogen-bonding interactions between active site residues.