In silico molecular targets, docking, dynamics simulation and physiologically based pharmacokinetics modeling of oritavancin

Table 3 Molecular docking result

S.N	Molecular targets	Oritavancin
S.N	Molecular targets	Binding affinity (kcal.mol^− 1)	Interacting amino acids residues
1	Cytochrome P450 3A4	−7.568	Hydrophobic forces: ASP174, VAL175, ALA178, PRO199, LEU211, ARG212, LYS487.
			Hydrogen bond: PRO199, ARG212, SER478A, GLY480, GLN484, GLU486.
			Salt bridges: LYS208, ARG212.
2	Cytochrome P450 2D6	−7.518	Hydrophobic forces: LEU213, LYS214, GLU215, VAL480, PRO489.
			Hydrogen bond: GLN52, SER217.
			π-Cation interactions: LYS214
			Halogen bond: SER217
			Salt bridges: LYS214
3	Cytochrome P450 2C9	−8.144	Hydrophobic forces: ARG132, PHE419, LYS421, LYS432, ALA439
			Hydrogen bond: GLY431, VAL436
			Halogen bonds: ARG342
4	Cytochrome P450 2C19	−8.384	Hydrophobic forces: ASP165, THR167, PHE168, LEU195, PHE482.
4	Cytochrome P450 2C19	−8.384	Hydrogen bond: GLU155, LYS158, LYS160A, ASP165, THR167.
5	PI3-kinase p110-gamma subunit	−10.34	Hydrophobic forces: LEU823, LEU865, VAL882
			Hydrogen bond: GLU301, HIS304, SER824, GLU826, ILE881, LYS883, ARG927, GLU956
			Salt bridges: LYS883, LYS920
6	Acyl-CoA desaturase	−10.07	Hydrophobic forces: TRP47, HIS57, PHE151, PHE152, PHE160, ILE230, LEU237, ALA241
			Hydrogen bond: TYR245
			π-stacking: TYR245
7	P-glycoprotein 1	−5.365	Hydrophobic forces: THR44, TYR46, ARG355
7	P-glycoprotein 1	−5.365	Halogen bonds: TYR51.

ISSN: 2050-6511