Harding Marjorie M
Institute of Cell and Molecular Biology, University of Edinburgh, Michael Swann Building, Edinburgh EH9 3JR, Scotland, UK.
Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):872-4. doi: 10.1107/s0907444902003712. Epub 2002 Apr 26.
In previous papers [Harding (2001), Acta Cryst. D57, 401-411, and references therein] the geometry of metal-ligand interactions was examined for six metals (Ca, Mg, Mn, Fe, Cu, Zn) using the Protein Data Bank and compared with information from accurately determined structures of relevant small-molecule crystals in the Cambridge Structural Database. Here, the environments of Na(+) and K(+) ions found in protein crystal structures are examined in an equivalent way. Target M(+).O distances are proposed and the agreement with observed distances is summarized. The commonest interactions are with water molecules and the next commonest with main-chain carbonyl O atoms.
在之前的论文中[哈丁（2001年），《晶体学报》D辑，第57卷，401 - 411页，以及其中的参考文献]，利用蛋白质数据库研究了六种金属（钙、镁、锰、铁、铜、锌）与配体相互作用的几何结构，并与剑桥结构数据库中相关小分子晶体精确测定结构的信息进行了比较。在此，以同样的方式研究了蛋白质晶体结构中发现的钠离子和钾离子的环境。提出了目标M⁺·O距离，并总结了与观测距离的一致性。最常见的相互作用是与水分子，其次是与主链羰基氧原子。
