Gold complexes as a new class of non-platinum antitumor drugs with prominent cytotoxic activities are presently being evaluated as potential anticancer agents.It was observed that the gold anticancer mechanism of action are through different pathways su ch as inhibition of the thioredoxinreductase (TrxR), selenium-glutathione peroxidase and gluthationereductase (GR) enzymes as well as intercalation with the DNA base pairs. Here, Molecular docking studies of Alkynyl(triphenylphosphine)gold(I) complexes, as novel anticancer gold(I) compounds were performed on three targets including TrxR, GR and DNA by means of AutoDock 4.2 to acquire the detailed molecular binding modes and binding sites for these compounds tothe above targets. The docking results indicated that the important amino acids inside the active site of the cavity that are responsible for essential interactions are Ile A52, Glu A54 and Arg B25 for TrxR andArg37, and Asn117 for GR receptors. A5, G4, G10 and C11 are among the most base pairs that involved in the interaction of these compounds to the DNA.