Table 3.
Thermodynamic parameters and interacting amino acid residues of the protein-ligand complexes formed between HsrA and selected DHP-based HHQ derivatives, according to ITC and molecular docking analyses.
| DHP | ITC1 | Molecular docking2 | ||
|---|---|---|---|---|
| Kd (μM) | ΔH (kcal/mol) | ΔG (kcal/mol) | Interacting residues | |
| MD1 | 3.5 | −1.5 | −7.4 | I135, V144, F149, L152, K194, M195, P198, L199 |
| MD2 | 16 | −3.1 | −6.5 | I135, Y137, V144, K145, G146, K194, P198 |
| MD6 | 25 | −2.0 | −6.3 | I135, Y137, V142, V144, P148, F149, L152, K194, P198, L199 |
| MD7 | 23 | −7.8 | −6.3 | I135, Y137, V142, V144, F149, L152, K194, M195, P198, L199 |
| HM4 | 4.0 | −0.7 | −7.4 | I135, Y137, V142, V144, G146, P148, F149, K194, P198 |
| HM6 | 5.4 | −2.7 | −7.2 | I135, Y137, V142, V144, G146, P148, K194, P198 |
1
Relative error in Kd is 15%, absolute error in ΔH is 0.4 kcal/mol, absolute error in ΔG is 0.1 kcal/mol.
2
Amino acid residues directly involved in forming the helix-turn-helix (HTH) DNA binding motif of HsrA are highlighted in bold fonts.