Table 4.
Analyses of the interaction between HsrA and its bactericidal inhibitors by isothermal titration calorimetry and molecular docking.
| Compound | ITCa | Molecular Dockingb |
|||
|---|---|---|---|---|---|
| n |
Kd (µM) |
ΔH (kcal/mol) |
ΔG (kcal/mol) |
Interacting residues | |
| chrysin | 0.77 | 17 | −4.1 | −6.5 | P181, K165, I184 |
| apigenin | 0.81 | 20 | −3.8 | −6.4 | P198, I135, K194, V144, G146, K145, L152 |
| hesperetin | 0.83 | 26 | −5.8 | −6.2 | P198, M195, I191, K194, P148, V144, K145, G146, L152 |
| kaempferol | 0.78 | 33 | −8.6 | −6.1 | Y137, K194, P148, G146 |
aAbsolute error in n is 0.06, relative error in Kd is 40%, absolute error in ΔH is 0.4 kcal/mol, absolute error in ΔG is 0.2 kcal/mol.
bAmino acid residues directly involved in forming the helix-turn-helix (HTH) DNA binding motif of HsrA are highlighted in bold fonts.