Breast cancer is the most common cause of cancer deaths in women. Normal breast cells and most breast cancer cells have receptors that attach to circulating estrogen and progesterone. Estrogen and progesterone bind to the receptors and may cause cancer cells to proliferate. Drugs, currently being used to treat this disease are not so effective and cause adverse effects. For this reason, the quest of new compounds that bind to the estrogen receptor (ER), activating or inhibiting ERs selectively, is a very active field of research. In this task, molecular docking plays a vital role in drug design, either as a tool in drug discovery and analysis of proteinligand interactions. In this work, 26 steroidal oximes, which are derivatives of diosgenin, were analyzed using docking studies, and compared against the estrogen receptor (ER alpha). The 3D structures of ER alpha were downloaded from Protein Data Bank (3ERT) and optimized using pdb2pqr.py. Modifications in rings A and B were made, and both oxime configurations (E or Z) were considered. Results for hydroximino steroids were compared with those obtained for compounds exhibiting biological activity against this type of cancer, namely, 4-hydroxytamoxifen, diosgenin and 6,23-dihydroximino diosgenin derivative. Molecular docking studies on ER alpha revealed that three mono oximes were found to interact with the protein more efficiently and have the best docking score. Thus, modification of diosgenin with oxime groups could lead to antiproliferative steroidal compounds, and therefore they could be considered for further research and in vivo evaluations for breast cancer treatment and management strategies.