Manganese (Mn) is an important metal that is crucial in biological cell mechanism and function. However, its binding mechanism is poorly characterized. In the present study, we have carried out a detailed statistical analysis of the Mn-containing proteins through analysis of the metal coordination spheres of the vast number of protein crystal structures present in Protein Data Bank. These results reveal that Mn metal predominantly acquires the coordination number of six and five. In these predominant six and five coordination spheres, Mn metal is majorly stabilized with octahedral and square pyramidal geometries respectively. The water molecules, aspartic acid, and glutamic acid residues bonded frequently with Mn metal ions. These results provided useful insights to characterize the very important Mn-containing subset of the proteome. Quantum mechanical results showed that the complexes with coordination number six are predominantly having high interaction energy, which is in good agreement with statistical analysis.

中文翻译：

---

蛋白质中锰金属配位的研究：综合 PDB 分析和量子力学研究

锰 (Mn) 是一种重要的金属，对生物细胞机制和功能至关重要。然而，其结合机制的特征很差。在本研究中，我们通过分析蛋白质数据库中存在的大量蛋白质晶体结构的金属配位球，对含锰蛋白质进行了详细的统计分析。这些结果表明，Mn 金属主要获得 6 和 5 的配位数。在这些主要的六个和五个配位球中，Mn 金属分别主要以八面体和四方锥体几何结构稳定。水分子、天冬氨酸和谷氨酸残基经常与锰金属离子结合。这些结果为表征蛋白质组中非常重要的含锰子集提供了有用的见解。