Table 1.
Docking Result Parameters of FBC with Normal 5-LOX Structure and its Four Homology Modeled Mutants. The Interacting Residues in All Proteins were Found to be Conserved with Atomic Distances ≤4.5 Å
| Protein | Binding Free Energy Kcal/mol |
Inhibition Constant Ki, μM |
Ligand Efficiency |
Intermolecular Energy |
Reference for Mutation |
Interacting Residues | Atomic Distance with FBC (Å) |
|---|---|---|---|---|---|---|---|
| 3O8Y | −8.54 | 0.545 | −0.24 | −10.33 | [33] | Arg246, Val361, Ala453, Val243, Leu244 | 2.2, 2.9, 2.4, 3.6, 4.05 |
| Cys562Ala | −7.91 | 1.58 | −0.23 | −9.7 | [33] | Arg264, Ala471, Arg264, Thr563, Val379, Leu306 | 2.25,2.79, 3.7, 3.2, 2.88, 2.88 |
| Cys241Ala | −8.76 | 0.376 | −0.26 | −10.07 | [33] | Val261, Val379, Leu466, Gln567, Arg388 | 3.3, 4.5, 3.5, 3.7, 3.43 |
| LysLysLys653-655GluAsnLeu | −8.38 | 0.725 | −0.24 | −10.17 | [33] | Leu306, Gln305, HOH733, Val261, Arg388, Gln567 | 4.9,3.87,2.7, 3.5, 3.7, 4.5 |
| Lys274Glu | −8.58 | 0.515 | −0.25 | −10.37 | [35] | Arg264, Leu262, Arg388, Gln567, Ala471 | 3.2, 3.0, 4.5, 4.5, 3.5 |