The serine/threonine kinase (Akt) plays a crucial role in regulating cell survival, proliferation, and apoptosis through the phosphoinositide 3-kinase (PI3K)/Akt/mTOR signaling pathway. Inhibiting Akt1, particularly its pleckstrin homology (PH) domain, is considered a key target for therapeutic interventions in various cancers. This study focuses on structure-based virtual screening (SBVS) of FDA-approved drugs targeting the Akt1 PH domain to identify potential inhibitors. Through comprehensive computational analyses, nine molecules were identified as promising candidates, exhibiting strong binding affinity and interactions with key residues at the Akt1 PH domain. Molecular dynamics simulations further confirmed the stability and favorable binding energies of the Akt1_179 (biotin) and Akt1_227 (lovastatin) complexes. These findings highlight the potential of repurposing FDA-approved drugs for cancer therapeutics, paving the way for further experimental validation and preclinical studies.