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 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.
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机译：三核锌配合物的结构，六（μ2-2-苯胺基苯并基）二水基三锌（II），[Zn2（C13H10NO2）6（H2O）2]或（NPA）6Zn3（H2O）2（NPA是2-苯胺基苯甲酸酯或N-苯基氨基苯胺酸盐），被报道。复合物在三斜空间群 P 中结晶，中心 ZnII 原子位于反转中心。发现 NPA 配体通过具有独特 C-O 键长度的羧酸盐 O 原子进行配位，该长度支持羧酸盐片段上共振的不均匀分布。轴向 H2O 配体与相邻分子形成氢键，这些分子将超分子系统稳定在刚性直链中，沿 c 轴呈 180° 角。π堆叠是沿 a 轴和 b 轴的主要稳定性，从而产生高度有序的超分子结构。对接研究表明，三核锌复合物的这种独特的超分子结构有可能与 SARS-CoV-2 中的主要蛋白酶 （Mpro） 结合，其位置与 Remdesivir不同，但具有相似的结合强度。
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