TP53 and breast carcinoma: Overall our results demonstrate that the structural features of interface atoms, surface atoms, interface residues, surface residues, interface SASA, total SASA, isolated structure Solvent energy, gain on complex formation, average gain in complex formation, number of hydrogen bonding residues and number of salt bridge residues are significant for predicting the impact of the mutations R110P, P278A and P151T induced by the deleterious breast cancer SNPs rs11540654, rs17849781 and rs28934874 predicted in our previous study [20] on the p53–ERα interaction.