At the end of the last century, it was revealed that quinones with one, two, and three aromatic rings could inhibit HIV-1 protease, an enzyme crucial for HIV (Human Immunodeficiency Virus) replication. Since HIV-1 protease acts as key target for AIDS medications (Acquired immunodeficiency syndrome), the development of efficient inhibitor of this protein would lead to the increasing of the medical treatment, and decreasing of the drug resistance. Later research revealed that simply hydroxyquinones can block HIV-1 protease at the micromolar level, which enabled a direction for the creation of HIV medications. Anthrarufin (1,5-dihydroxy-9,10-anthraquinone) is an anthraquinone that posses a moderate antioxidative capacity and antimalaric activity. In this study, molecular docking simulations were used to examine the molecular interactions between anthrarufin, its monoanion and dianion as ligands, and the HIV-1 reverse transcriptase (HIV-1 RT) as target protein. Using AGFR software, the binding site of the HIV-1 RT is identified. The three-dimensional crystal structure of HIV-1 RT is downloaded from the Protein Data Bank (PDB ID: 2ZD1). Dolutegravir, nevirapine, anthrarufin, anthrarufin-anion and anthrarufin-dianion are used as ligands in the molecular docking simulations together with rilpivirine (TMC278), a non-nucleoside inhibitor of estimated protein. The AutoDock 4.0 program is used for molecular docking simulations. Anthrarufin, its monoanion and dianion can be considered as a potential HIV-1 RT inhibitors because they have similar inhibitory potency to other ligands under consideration, according to the results of the free energy of binding (∆G_bind) and inhibition constant (K_i) values.