Table 4.
Interacting residues of PKA with Dactinomycin, Temsirolimus, Everolimus, Docetaxel, and Bromocriptine.
| Drugs | Binding Affinity (−log10(KD|Ki)) | Protein Residue | Distance (Å) | Type of Interactions |
|---|---|---|---|---|
| Dactinomycin | 39.1 | PHE 54 | 3.03 | Hydrophobic |
| VAL 57 | 3.92 | Hydrophobic | ||
| LYS 72 | 3.55 | Hydrophobic | ||
| LEU 82 | 3.95 | Hydrophobic | ||
| GLU 170 | 3.57 | Hydrophobic | ||
| PHE 187 | 3.74 | Hydrophobic | ||
| PRO 202 | 3.93 | Hydrophobic | ||
| THR 51 | 2.12 | H-bond | ||
| SER 53 | 2.34 | H-bond | ||
| LYS 168 | 5.13 | Salt bridge | ||
| Temsirolimus | 35.5 | PHE 54 | 3.35 | Hydrophobic |
| VAL 57 | 3.32 | Hydrophobic | ||
| PHE 129 | 3.26 | Hydrophobic | ||
| PRO 202 | 3.72 | Hydrophobic | ||
| THR 51 | 2.47 | H-bond | ||
| LYS 72 | 2.33 | H-bond | ||
| LYS 168 | 2.56 | H-bond | ||
| LYS 168 | 5.48 | Salt bridge | ||
| Everolimus | 37.3 | PHE 54 | 3.21 | Hydrophobic |
| PHE 129 | 3.43 | Hydrophobic | ||
| GLU 170 | 3.72 | Hydrophobic | ||
| THR 51 | 3.96 | Hydrophobic | ||
| SER 53 | 3.28 | H-bond | ||
| ARG 133 | 1.94 | H-bond | ||
| LYS 168 | 3.18 | H-bond | ||
| Docetaxel | 38.2 | PHE 54 | 3.25 | Hydrophobic |
| VAL 57 | 3.52 | Hydrophobic | ||
| LEU 74 | 3.52 | Hydrophobic | ||
| PHE 129 | 3.21 | Hydrophobic | ||
| PHE 187 | 3.34 | Hydrophobic | ||
| PRO 202 | 3.73 | Hydrophobic | ||
| TYR 330 | 3.84 | Hydrophobic | ||
| LYS 168 | 2.39 | H-bond | ||
| GLU 170 | 3.17 | H-bond | ||
| LYS 72 | 4.87 | Pi-stacking | ||
| LYS 168 | 4.86 | Salt bridge | ||
| Bromocriptine | 33.8 | PHE 54 | 3.78 | Hydrophobic |
| LYS 72 | 3.45 | Hydrophobic | ||
| LEU 74 | 3.52 | Hydrophobic | ||
| GLU 170 | 3.84 | Hydrophobic | ||
| THR 51 | 2.66 | H-bond | ||
| LYS 72 | 1.59 | H-bond | ||
| LYS 168 | 3.70 | Salt bridge | ||
| GLU 170 | 5.34 | Salt bridge |