Acyclovir is a widely used antiviral drug effective against herpes simplex virus (HSV) infections. To elucidate the molecular basis of its antiviral activity, we performed molecular docking studies to investigate the interaction of acyclovir with the HSV DNA polymerase enzyme, a critical target for antiviral therapy. The 3D structure of the HSV DNA polymerase was retrieved from the Protein Data Bank (PDB), and the structure of acyclovir was obtained from PubChem. Using Auto Dock Vina, we conducted docking simulations to predict the binding orientation and affinity of acyclovir to the active site of the DNA polymerase. The docking results revealed that acyclovir binds effectively to the DNA polymerase with a high affinity, forming several key interactions, including hydrogen bonds and hydrophobic contacts. These interactions are consistent with the mechanism of action of acyclovir, where it acts as a chain terminator during viral DNA replication. The binding affinity scores and interaction profiles were analysed and visualized using PyMOL, providing insights into the specific residues involved in binding and the potential conformation changes upon drug binding. This study enhances our understanding of the molecular interactions between acyclovir and HSV DNA polymerase, supporting its role in inhibiting viral replication. These findings may guide the design of improved antiviral agents and the development of strategies to combat HSV infections more effectively.