Table 4. The binding energy (ΔG_bind) in kcal mol⁻¹, inhibition constant (K_i), and amino acid residue–ligand interactions for the selected compounds and standard drug ketoconazole targeting 14α-sterol demethylase (CYP51) (PDB ID: 1EA1).

Ligand compound	ΔGbind	K i a (µM)	Amino acid residual (interactions)
3	−8.20	0.98	Pro320(Hydrogen bond), Ile322(π–alkyl), Leu321(π–alkyl), Tyr76(π–π T-shaped), Phe78(π–π T-shaped), Met79 (π–sulphur, π–alkyl), Met433(π–lone pair), Phe255(van der Waals), Val435(van der Waals), Val434(van der Waals), His259(van der Waals), Ile323(van der Waals)
5	−8.38	0.72	Met433(π–lone pair), Ile322(π–alkyl), Val435(π-alkyl), Leu321(π-alkyl), Val434(π-alkyl), Met79(π-alkyl), Phe78(π– π T-shaped), Ile323(π-donor hydrogen bond)), Phe255(van der Waals), His259(van der Waals), Pro320(van der Waals), Tyr76 (van der Waals)
6	−7.22	5.13	Ser252(Hydrogen bond), Leu100(π-alkyl), Met99 (π-alkyl), Ala256(π-alkyl), Leu321 (π-alkyl), Hem460(π-alkyl), Phe83(π– π T-shaped), Arg96(van der Waals), Phe255(van der Waals), Met253(van der Waals)
Ketoconazole	−9.45	0.12	Arg96(Hydrogen bond), Thr80(Carbon hydrogen bond), Gly84(Carbon hydrogen bond), Phe83(π–π T-shaped), Phe78(π–π T-shaped), Met79(π–alkyl), Leu321(alkyl, π–alkyl), Val434(alkyl), His259(alkyl), Tyr76(π–sigma), Met433(van der Waals), Phe255(van der Waals), Hem460(van der Waals), Ala256(van der Waals),Met99(van der Waals)

^a K _i = exp(ΔG/RT), where R = 1.985 × 10⁻³ kcal mol⁻¹ K⁻¹ and T = 298.15 K.