In the present paper nine molecules has been docked in the Acyl-CoA carboxylasecarboxyltransferase domain 5 (AccD5) at GLY-193, GLY-194, GLY-434, ALA-435 pocket with very lowenergies. Six binding site on the crystallographic structure of AccD5 are examined with the structure-baseddesign program DOCK. The active compounds found are polycyclic (aromatic as well as aliphatic) andnitrogen heterocyclic. Each molecule gave a good number of conformations showing the flexible behavior ofthe ligand. The total energy of receptor-ligand complexes has also been calculated.