Docking studies of staurosporine and three inhibitor molecules with the isoquinolinesulphonamide structure, H7, H8 and H89, were performed to cAMP-dependent protein kinase, in order to interpret their competitivity between them and ATP. The crystal structure of the enzyme complexed with a peptidyl inhibitor, ATP and Mn^<2+> was taken from PDB. The program ADAM, which was developed for searching stable docking models automatically covering all possible binding modes and ligand conformations, was used for this purpose. Inter- and intramolecular energies were used in all pruning steps of the program and several stable models were yielded from the program. For each inhibitor molecule, the most stable docking model, which was obtained after energy minimization of the models considering protein flexibilities and water molecules, was used for later discussion. Based on these docking models, the complicated inhibitory behaviors of the molecules were well explained by the spaces in the active site of the enzyme occupied by them.