Table 3.
Interactions of amino acid residues with EXP3174 at receptor sites of MPro and RBD of S protein of SARS-CoV-2 using PLIP. Binding energies and affinity constants should be viewed in relative terms—they highlight differences between ligands and do not account for entropy differences.
| Type of Interactions | Amino Acids of Mpro Involved and Distance of Interactions (A°) | |
|---|---|---|
| Hydrogen Bonds | Leu141 | 1.91 |
| Ser144 | 3.40 | |
| His163 | 2.00 | |
| His172 | 3.61 | |
| Thr190 | 2.09 | |
| Thr190 | 1.86 | |
| Gln192 | 1.98 | |
| Hydrophobic Interactions | Met165 | 3.25 |
| Glu166 | 3.97 | |
| Pro168 | 3.82 | |
| π-Stacking (Stacking Type T) | His163 | 4.11 |
| Halogen Bonds | Gln192 | 3.61 |