Two S-benzyl substituted carbodithioates –namely benzyl benzylmethylcarbamodithioate (1) and 4-(trifluoromethyl)benzyl azepane-1-carbodithioate (2)– were synthesized by a single pot three-component reaction. Structures 1 and 2 were elucidated by means of FTIR, 1H-NMR, 13C-NMR, and single-crystal XRD analyses. Single crystal X-ray studies combined with Hirshfeld surface analysis manifestations outlined the opulent contributions of the intramolecular C-H⋯S interaction in stabilizing the molecular configuration of both compounds. Both carbodithioates under study showed encouraging indications for inhibition efficiency toward urease enzyme, with 1 (IC50 = 0.75 ± 0.04 μM) being more efficient than 2 (IC50 = 1.22 ± 0.02 μM), respectively. Docking computations revealed the binding modes of 1 and 2 with the targeted enzymes. The presented work would serve as a cornerstone for future investigations into potential new inhibitors for pharmaceutical and biological applications.