Table 8. The interaction energy of phenolic compounds toward AChE anionic site.
| Residue | IE | VDW | Electrostatics | Residue | IE | VDW | Electrostatics |
|---|---|---|---|---|---|---|---|
| (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | ||
| AChE | |||||||
| Anionic site | |||||||
| 1 | 2 | ||||||
| TYR 71 | -0.79 | -2.41 | 1.62 | TYR 71 | 0.41 | -0.78 | 1.19 |
| GLU 80 | -0.69 | -1.75 | 1.06 | GLU 80 | -6.62 | -1.43 | -5.19 |
| TRP 83 | -5.3 | -5.034 | -0.27 | TRP 83 | -6.31 | -6.82 | 0.51 |
| ASN 84 | -2.51 | -1.53 | -0.98 | ASN 84 | -1.96 | -2.35 | 0.39 |
| TYR 148 | -4.18 | -0.2 | -3.99 | TYR 148 | -3.66 | -0.83 | -2.83 |
| GLY 149 | -1.8 | -1.21 | -0.59 | GLY 149 | -0.075 | -1.51 | 1.43 |
| GLY 150 | -2.64 | -1.87 | -0.76 | GLY 150 | -1.93 | -2.3 | 0.37 |
| GLY 151 | 0.68 | -0.24 | 0.91 | GLY 151 | 0.52 | -0.23 | 0.75 |
| THR 154 | -0.99 | -1.42 | 0.43 | THR 154 | -2.8 | -2.27 | -0.53 |
| GLY 155 | -0.24 | -0.36 | 0.12 | GLY 155 | -2.42 | -0.98 | -1.44 |
| SER 156 | -1.25 | -0.096 | -1.16 | SER 156 | -2.86 | -0.63 | -2.23 |
| TYR 162 | -0.9 | -0.51 | -0.38 | TYR 162 | -4.93 | -1.48 | -3.45 |
| GLU 237 | -6.71 | -0.83 | -5.88 | GLU 237 | -2.15 | -0.45 | -1.7 |
| SER 238 | -3.18 | -0.85 | -2.33 | SER 238 | -2.24 | -0.35 | -1.88 |
| TYR 370 | -2.13 | -1.98 | -0.15 | TYR 370 | -3.33 | -1.48 | -1.84 |
| PHE 371 | -1.26 | -0.36 | -0.9 | PHE 371 | 0.36 | -0.31 | 0.67 |
| TRP 472 | 1.78 | -0.22 | 2 | TRP 472 | -1.84 | -0.31 | -1.53 |
| HIS 480 | -2.19 | -1.24 | -0.95 | HIS 480 | 1.13 | -0.65 | 1.78 |
| ILE 484 | -2.5 | -0.48 | -2.03 | ILE 484 | -0.53 | -0.37 | -0.16 |
| 3Å IE | -31.43 | -20.60 | -10.83 | 3Å IE | -36.49 | -22.86 | -13.62 |
| Total IE | -80.74 | -26.569 | -54.18 | Total IE | -118.32 | -29.94 | -88.38 |
Note: The bold amino acid residues of AChE are involved in 3Å vicinity of compound upon binding.