The molecular structures of some dichlorodiorgano[N-(2-pyridylmethylene)arylamine]tin(IV) (R2SnCl2.L) complexes were determined using the PM3 method and their geometries have been optimized. The Sn atom in the complexes adopt a trans-R2Sn octahedral geometry. The mechanism for cytotoxic activities of some diorganotin(IV) compounds, R2SnCl2.L (R = Me (1), Et (2), Ph (4)) is discussed in relations to their docking in some of the cancer associated enzymes such as ribonucleotide reductase (RNR), thymidylate synthase (TS), thymidylate phosphorylase (TP) and topoisomerase II (topoII). The docking studies revealed that compound 1 docked in the active site of enzymes by virtue of hydrophobic interactions and comparable interactions were also noted for compound 2. On the other hand, compound 3 exhibited hydrogen bonding, hydrophobic and π-π interactions when docked to enzymes RNR, TS and topoII, respectively. None of the compounds entered the active site pocket of thymidylate phosphorylase (TP).
