Table 3.
Interacting residues of AMPA with Dactinomycin, Temsirolimus, Paclitaxel, Vincristine, and Irinotecan.
| Drugs | Binding Affinity (−log10(KD|Ki)) | Protein Residue | Distance (Å) | Type of Interactions |
|---|---|---|---|---|
| Dactinomycin | 37.1 | LEU 410 | 3.91 | Hydrophobic |
| TYR 450 | 3.29 | Hydrophobic | ||
| LEU 498 | 2.54 | Hydrophobic | ||
| LEU 650 | 3.87 | Hydrophobic | ||
| SER 654 | 2.75 | H-bond | ||
| THR 655 | 2.13 | H-bond | ||
| GLU 705 | 2.80 | H-bond | ||
| Temsirolimus | 38.2 | GLU 402 | 3.90 | Hydrophobic |
| TYR 450 | 3.65 | Hydrophobic | ||
| PRO 478 | 478 | Hydrophobic | ||
| THR 482 | 3.93 | Hydrophobic | ||
| PRO 494 | 2.99 | Hydrophobic | ||
| LEU 498 | 2.78 | Hydrophobic | ||
| GLU 705 | 3.77 | Hydrophobic | ||
| MET 708 | 2.32 | Hydrophobic | ||
| LYS 730 | 3.30 | Hydrophobic | ||
| TYR 732 | 3.85 | Hydrophobic | ||
| SER 654 | 2.82 | H-bond | ||
| GLU 705 | 2.98 | H-bond | ||
| GLY 731 | 2.89 | H-bond | ||
| Paclitaxel | 36.1 | TYR 405 | 3.03 | Hydrophobic |
| TYR 450 | 3.80 | Hydrophobic | ||
| THR 480 | 3.56 | Hydrophobic | ||
| LEU 498 | 3.66 | Hydrophobic | ||
| PHE 658 | 3.71 | Hydrophobic | ||
| GLU 705 | 3.29 | Hydrophobic | ||
| LYS 730 | 3.00 | Hydrophobic | ||
| SER 654 | 2.42 | H-bond | ||
| THR 686 | 2.77 | H-bond | ||
| Vincristine | 34.4 | GLU 402 | 3.56 | Hydrophobic |
| TYR 450 | 3.11 | Hydrophobic | ||
| LEU 650 | 3.38 | Hydrophobic | ||
| PHE 658 | 3.99 | Hydrophobic | ||
| LYS 730 | 3.01 | Hydrophobic | ||
| SER 654 | 1.74 | H-bond | ||
| THR 655 | 3.15 | H-bond | ||
| THR 686 | 1.87 | H-bond | ||
| GLU 705 | 2.66 | H-bond | ||
| TYR 732 | 2.95 | H-bond | ||
| Irinotecan | 35.1 | GLU 402 | 2.71 | Hydrophobic |
| TYR 450 | 3.03 | Hydrophobic | ||
| THR 480 | 3.47 | Hydrophobic | ||
| LEU 498 | 3.35 | Hydrophobic | ||
| GLU 705 | 3.02 | Hydrophobic | ||
| MET 708 | 2.22 | Hydrophobic | ||
| LYS 730 | 3.55 | Hydrophobic | ||
| THR 686 | 1.80 | H-bond | ||
| TYR 450 | 3.52 | Pi-stacking |