The emergence of drug resistant strains of Plasmodium spp. creates a critical need for the development of Novel antimalarial. Formation of hemozoin, a crystalline heme detoxification process vital to parasite survival serves as an important drug target. Docking of indolo [3,2-c]quinolones complexes with 3DGA (wild type Plasmodium falciparum di hydrofolate reductage-thymidylate synthase [pf-DHFR-TS] complexed with RJF01320, NADPX and DUMP was performed to gain insight into the structural requirements and preferred conformations of these inhibitors. The study was conducted on a selected set of 100 compounds with variation in structure and activity. We found that the most active compounds established three hydrogen bonds, but some of the less active compounds have other binding modes. The application of docking study allowed conclusions to be drawn for the choice of suitable β-hematin inhibitors