Table 1. AutoDock binding energy values and H-bond forming residues of the lead molecules.
| COX-1 | COX-2 | |||
| Ligands | AutoDock Binding Energy | H-bond Forming Residues | AutoDock Binding Energy | H-bond Forming Residues |
| Amarogentin | −7.67 | Arg119, Ser352 | −10.32 | Tyr371, Ser516, Arg106, Met508 |
| Aspirin | −5.91 | Ser529, Tyr347 | −6.03 | Ser516 |
| Celecoxib | −8.37 | Tyr384, Ser529, Tyr347 | −8.6 | Ser516, Ser339 |
| Diclofenac | −7.19 | Tyr347 | −7.45 | Ser516, Tyr371 |
| Etodolac | −7.87 | Ser529 | −7.19 | Ser339 |
| Etoricoxib | −8.8 | Tyr347 | −10.41 | Arg499 |
| Flurbiprofen | 8.76 | Arg119 (2 H Bonds) | −8.61 | Arg106, Tyr341 |
| Ibuprofen | −7.81 | Arg119 (2 H Bonds) | −7.34 | Trp373, Phe367 |
| Indometacin | −5.12 | Tyr354, Ile522 | −8.35 | Tyr341 |
| Ketoprofen | −9.04 | Tyr384, Arg119 | −8.81 | Ser516, Ala513, Met508 |
| Ketorolac | −8.08 | Arg119 (2 H Bonds) | −8.45 | Trp373 |
| Lumiracoxib | −7.05 | Arg119 (2 H Bonds) | −8.17 | Ser516 |
| Meloxicam | −8.13 | None | −10.29 | Tyr371 (2 H bonds) |
| Nabumetone | −8.13 | Arg375 | −8.67 | Tyr371 |
| Naproxen | −7.88 | Arg375 | −8.24 | Tyr371, Arg106 |
| Nimesulide | −8.69 | Ala201, Tyr347, Ser529 | −9.51 | Tyr371, Ser516 |
| Parecoxib | −10.73 | Ser529 | −11.67 | Ser339, Val335 |
| Piroxicam | −8.29 | Ser529 | −9.6 | Ser516, Ser339, Ala513, Val 509 |
| Rofecoxib | −9.45 | Tyr347 | −9.72 | Tyr371, Trp373 |
| Sulindac | −6.75 | Tyr347 | −9.87 | Phe367 |
| Tolmetin | −7.92 | Arg119 (2 H bonds) | −8.09 | Trp373, Ser516 |
| Valdecoxib | −8.8 | Ser529, Phe528, Tyr347 | −9.51 | Ser339 (2 H bonds), Val335 |
Docking prediction of high scoring poses of different COX inhibitors and their corresponding binding energy values was compared with the binding free energy of amarogentin. Subsequently, the H-bonding residues were also analysed for the stability of the docking poses.