Table 1. Interactions of bilastine with the active site of RdRp.
|
Functional group |
Residue |
Bond |
Distance (Å) |
|
Carboxylic acid |
Asp761 |
H-bond (A-B) |
2.26 |
|
Carboxylic acid |
Ser814 |
H-bond (D-B) |
2.43 |
|
Ethoxy |
Asp623 |
H-bond (D-S) |
2.25 |
|
Ethoxy |
Cys622 |
H-bond (D-S) |
2.27 |
|
Benzimidazole |
Arg553 |
Electrostatic/pi-cation |
4.27 |
|
Benzimidazole |
Arg553 |
Electrostatic/pi-cation |
4.32 |
|
Benzimidazole |
Lys621 |
Electrostatic/pi-cation |
4.94 |
|
Benzimidazole |
Lys621 |
Electrostatic/pi-cation |
4.78 |
|
Benzimidazole |
Arg624 |
Hydrophobic/pi-alkyl |
5.34 |
|
Ethoxy |
Asp760 |
Carbon hydrogen bond |
3.49 |
|
Ethoxy |
Cys622 |
Hydrophobic/alkyl-alkyl |
3.82 |
For amino acid, A: H-bond acceptor, D: H-bond donor, B: Backbone interaction, S: Sidechain interaction. Light green: Carbon hydrogen bond, Green: H-bond, Orange: Electrostatic interactions, Pink: Hydrophobic interactions, RdRp: RNA-dependent RNA polymerase