Table 4.
Calculated interactions and affinities of compounds 1–3 with active-site residues of the Staphylococcus Gyr-B and PK.
| Protein Target | Ligand | IC50 (µM) * | Binding Energy (kcal/mol) | Hydrogen Bonding Interactions | Hydrophobic Interactions |
|---|---|---|---|---|---|
| Gyr-B | 1 | 19.18 ± 1.69 | −7.6 | ASN-54, GLU-58 | ILE-51, VAL-79 PRO-87, ILE-86 ILE-102, ILE-103 ILE-175 |
| 2 | 21.28 ± 2.36 | −7.5 | SER-55, ILE-51 | ILE-51, VAL-79 PRO-87, ILE-86 ILE-102, ILE-103 ILE-175 |
|
| 3 | 27.69 ± 1.08 | −7.2 | SER-55, ILE-51 | ILE-51, VAL-79 PRO-87, ILE-86 ILE-102, ILE-103 ILE-175 |
|
| Co-crystallized ligand | 0.091 | - | ASP-81, ASN-54 | ILE-51, VAL-79 PRO-87, ILE-86 ILE-102, ILE-103 ILE-175 |
|
| PK | 1 | 7.2 ± 0.07 | −7.7 | SER-362A, SER-362B THR-366A, THR-353B, ASN-369A |
ALA-358B, ILE-361B, LEU-370A |
| 2 | 9.3 ± 0.03 | −7.5 | SER-362A, THR-366A, THR-353B, ASN-369A | ALA-358B, ILE-361B, LEU-370A |
|
| 3 | 22.5 ± 0.04 | −6.5 | ASN-369B, THR-353A | ALA-358A, ILE-361A | |
| Co-crystallized ligand | 0.24 | - | SER-362A, SER-362B, ASN-369B, HIS-365A | ALA-358A, ALA-358B ILE-361B, LEU-370A |
* IC50 ± SD (µM).