Table 1.
The binding affinity results of molecular docking. If the pKd is large, then the binding affinity is increased. If ΔG is negative, then ligand and protein can be combined. Kd, equilibrium dissociation constant; pKd, −log (Kd); ΔG, Gibbs free energy; ARH, 3-(hydroxymethyl)-1-methyl-5-(2-methylaziridin-1-yl)-2-phenyl-1h-indole-4,7-dione (Pubchem CID: 5287703); FAD, Flavin-adenine dinucleotide (Pubchem CID: 643975).
| Ligand Name | Molecular Weight | pKd | ΔG (kcal/mol) |
|---|---|---|---|
| Fusarubin | 306.07 | 7.8 | −10.53 |
| ARH | 322.13 | 7.55 | −10.19 |
| FAD | 785.16 | 6.8 | −9.18 |