Compound 1 docks into αIIbβ3 with a more favorable interaction energy than into αVβ3
| Receptor-antagonist complex (PDBID)* . | Compound 1 docking energies . | Percentage of solutions with similar orientation‖ . | ||
|---|---|---|---|---|
| Total† . | van der Waals‡ . | Electrostatic§ . | ||
| αIIbβ3-tirofiban (1TY5) | −91.6 | −31.5 | −60.1 | 75 |
| αIIbβ3-eptifibatide (1TY6) | −92.1 | −31.4 | −60.7 | 65 |
| αVβ3-cilengitide (cyclic RGD, 1L5G) | −73.0 | −12.2 | −60.9 | 55 |
| Receptor-antagonist complex (PDBID)* . | Compound 1 docking energies . | Percentage of solutions with similar orientation‖ . | ||
|---|---|---|---|---|
| Total† . | van der Waals‡ . | Electrostatic§ . | ||
| αIIbβ3-tirofiban (1TY5) | −91.6 | −31.5 | −60.1 | 75 |
| αIIbβ3-eptifibatide (1TY6) | −92.1 | −31.4 | −60.7 | 65 |
| αVβ3-cilengitide (cyclic RGD, 1L5G) | −73.0 | −12.2 | −60.9 | 55 |
Receptor-antagonist complex used in the docking experiment and its corresponding Protein Data Bank entry.
Total energy of interaction (kcal/mol) of compound 1 in the best-scored docking orientation. This is the sum of van der Waals and electrostatic forces.
Van der Waals contributions to the docking energy (kcal/mol).
Electrostatic contribution to the docking energy (kcal/mol).
Percentage of solutions (of 20 best-scored) belonging to the most populated group of solutions (cutoff 2 Å RMSD).