The molecular docking study was conducted to investigate the binding interactions of 6-gingerol with fungal targets, focusing on its potential as antifungal agent. Binding affinities of the compounds ranged from -5.5 to -8.2 kcal/mol, reflecting varying degrees of interaction strength with the target proteins. Among the tested compounds, N-myristoyltransferase exhibited the highest binding affinity (-8.2 kcal/mol), forming hydrogen bonds with Tyr-335 and Leu-451 and engaging in hydrophobic interactions with residues such as Phe-115, His-227, Phe240, Phe-339, Ile-352, Tyr-354, Leu-394, Leu-415. Van der Waals interactions with Ile-111, Tyr-225, Leu-350, Val-390 Cys-393, Asn-392, Val-449, Leu-450 further enhanced its stability within the binding pocket (Figure ). The docking scores indicate moderate to strong binding efficiency for 6-gingerol. These findings emphasize the role of hydrogen bonds and hydrophobic interactions in stabilizing ligand-protein complexes, with N-myristoyltransferase emerging as the most potential target. Further experimental validation, such as enzyme inhibition assays and molecular dynamics simulations, is necessary to confirm the biological activity 6-gingerol. The binding affinity, hydrogen bonds, and residual interactions for all are summarized in Table .