Table 2.
Hydrogen bonding interactions between TMPRSS2 and Camostat mesylate, Nafamostat and Bromhexine hydrochloride after molecular docking.
| Sr. No. | Interactions between active site residues of TMPRSS2 with Camostat mesylate. | Distance in Å |
|---|---|---|
| 1 | Asp 345 OD2 ------ Lig. 1.A H: | 1.92 |
| Ser 441 HG ------ Lig. 1.A O: | 1.94 | |
| 2 | Ser 441 HN ------ Lig. 1.A O: | 2.21 |
| 3 | ||
| 4 | Tyr 337 OH ------ Lig. 1.A H: | 3.07 |
| 5 | Gly391 O ------ Lig. 1.A C: | 3.73 |
| Sr. No. | Interactions between active site residues of TMPRSS2 with Nafamostat. | Distance in Å |
| 1 | Gln 438 O ------ Lig. 1.A H: | 1.79 |
| 2 | Gln 317 O ------ Lig. 1.A H: | 2.17 |
| 3 | Gln 438 OE1 ------ Lig. 1.A H: | 3.12 |
| Sr. No. | Interactions between active site residues of TMPRSS2 with Bromhexine hydrochloride. | Distance in Å |
| 1 | Thr 393 OG ------ Lig. 1.A H: | 2.26 |
| 2 | Thr 393 OG ------ Lig. 1.A H: | 2.51 |
| 3 | Asp 440 OD2 ------ Lig. 1.A C: | 3.35 |