Abstract Matrix metalloproteinase (MMPs) are a family of calcium‐dependent zinc‐containing endopeptidases which are responsible for the tissue remodeling and degradation of the extracellular matrix (ECM), including collagens, elastins, gelatin, matrix glycoproteins, and proteo‐ glycan. In this study, by using molecular docking and 3D‐QSAR analysis we get new insights into the relationship between experimental IC 50 values and their descriptors obtained from CoMSIA and CoMFA programs. Obtained information on molecular structural of a series of β‐N‐biaryl ether sulfonamide hydroxamates as potential MMP inhibitors, that can be used to understand the drug receptor interactions of these kind of molecules.