Table 2.
Molecular docking results of compounds (IVa–n)
| Comp. | Binding energy, kcal/mol |
Inhibition constant, nanomolar |
No. of hydrogen bonds |
Residues involved in hydrogen bonding (bond length in Å) |
π–π Stacking |
|---|---|---|---|---|---|
| (IVa) | –11.18 | 6.39 | 2 |
LYS721 (2.00), MET769 (2.34) |
LYS721 π cation |
| (IVb) | –11.82 | 2.18 | 2 |
LYS721 (2.00), MET769 (2.36) |
LYS721 π cation |
| (IVc) | –10.71 | 32.40 | 3 |
LYS721 (1.98), ARG817 (2.23), ASN818 (2.57) |
PHE699, ARG817 and ARG817 π cation |
| (IVd) | –12.03 | 1.53 | 2 | MET769 (2.50) | LYS721 π cation |
| (IVe) | –10.99 | 8.76 | – | – | – |
| (IVf) | –11.04 | 8.05 | 1 | LYS721 (2.22) | – |
| (IVg) | –10.96 | 14.15 | 1 | LYS721 (2.17) | PHE699, ARG817 |
| (IVh) | –11.02 | 8.01 | 3 |
ARG817 (1.72), ARG817 (2.79), LYS851 (2.32) |
TRP856, LYS721 π cation |
| (IVi) | –11.11 | 7.24 | 5 |
ALA698 (2.10), LYS721 (2.06), ARG817 (1.91), ARG817 (2.64), ASN818 (2.07) |
PHE699, ARG817 and LYS 852 formed salt bridge |
| (IVj) | –10.79 | 12.26 | 1 | LYS721 (2.30) | – |
| (IVk) | –9.57 | 97.04 | – | – | TRP856, ARG817 π cation and LYS851 π cation |
| (IVl) | –10.95 | 9.39 | 1 | LYS721 (1.64) | – |
| (IVm) | –10.95 | 9.43 | 2 |
LYS721 (2.23), PHE832 (2.15) |
LYS721 π cation |
| (IVn) | –10.17 | 35.22 | – | – | – |