The structure of a trinuclear zinc complex, hexakis(μ2-2-anilinobenzoato)diaquatrizinc(II), [Zn2(C13H10NO2)6(H2O)2] or (NPA)6Zn3(H2O)2 (NPA is 2-anilinobenzoate or N-phenylanthranilate), is reported. The complex crystallizes in the triclinic space group P\overline{1} and the central ZnII atom is located on an inversion center. The NPA ligand is found to coordinate via the carboxylate O atoms with unique C—O bond lengths that support an unequal distribution of resonance over the carboxylate fragment. The axial H2O ligands form hydrogen bonds with neighboring molecules that stabilize the supramolecular system in rigid straight chains, with an angle of 180° along the c axis. π stacking is the primary stabilization along the a and b axes, resulting in a highly ordered supramolecular structure. Docking studies show that this unique supramolecular structure of a trinuclear zinc complex has potential for binding to the main protease (Mpro) in SARS-CoV-2 in a different location from Remdesivir, but with a similar binding strength.