Table 6. The interaction energy of phenolic compounds toward AChE catalytic site.
| Residue | IE | VDW | Electrostatics | Residue | IE | VDW | Electrostatics |
|---|---|---|---|---|---|---|---|
| (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | (kcal/mol) | ||
| AChE | |||||||
| CAS site | |||||||
| 1 | 2 | ||||||
| ARG 70 | 2.02 | -0.083 | 2.1 | ARG 70 | -1 | -0.073 | -0.93 |
| TYR 71 | -6.27 | -3.34 | -2.93 | TYR 71 | -4.23 | -3.39 | -0.88 |
| GLU 80 | 3.29 | -1.52 | 4.81 | GLU 80 | -1.41 | -1.86 | 0.45 |
| TRP 83 | -3.08 | -2.72 | -0.37 | TRP 83 | -2 | -1.86 | -0.14 |
| GLY 149 | -1.2 | -0.84 | -0.36 | GLY 149 | -1.39 | -1.64 | 0.24 |
| GLY 150 | -0.34 | -1.16 | 0.82 | GLY 150 | 2.98 | 0.51 | 2.47 |
| GLY 151 | 0.14 | -0.85 | 0.99 | GLY 151 | -0.11 | -0.82 | 0.71 |
| THR 154 | -0.85 | -0.46 | -0.38 | THR 154 | -0.35 | -0.54 | 0.19 |
| TYR 162 | 2.22 | -0.38 | 2.6 | TYR 162 | 1.66 | -0.47 | 2.14 |
| GLU 237 | -1.32 | -0.32 | -1 | GLU 237 | -0.0037 | -0.55 | 0.55 |
| SER 238 | -2.81 | -0.38 | -2.43 | SER 238 | -2.81 | -0.82 | -1.99 |
| TYR 370 | -1.46 | -1.97 | 0.51 | TYR 370 | -5.04 | -2.18 | -2.86 |
| PHE 371 | -2.45 | -1 | -1.45 | PHE 371 | -0.81 | -1.49 | 0.69 |
| TYR 374 | -2.85 | -1.4 | -1.45 | TYR 374 | 2.08 | -1.5 | 3.58 |
| TRP 472 | -1.24 | -0.87 | -0.37 | TRP 472 | -1 | -0.95 | -0.045 |
| HIS 480 | -1.05 | -0.67 | -0.38 | HIS 480 | -2.77 | -1.25 | -1.52 |
| GLY 481 | -2.05 | -0.35 | -1.7 | GLY 481 | -1.57 | -0.4 | -1.17 |
| ILE 484 | -1.32 | -0.2 | -1.13 | ILE 484 | -2.47 | -0.31 | -2.16 |
| 3Å IE | -14.26 | -14.83 | 0.56 | 3Å IE | -16.51 | -17.25 | 0.71 |
| Total IE | -83.21 | -21.27 | -61.93 | Total IE | -100.29 | -22.81 | -77.48 |
Note: The bold amino acid residues of AChE are involved in 3Å vicinity of compound upon binding.