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Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):872-4. Epub 2002 Apr 26.

Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium.

Author information

1
Institute of Cell and Molecular Biology, University of Edinburgh, Michael Swann Building, Edinburgh EH9 3JR, Scotland, UK. marjorie.harding@ed.ac.uk

Erratum in

  • Acta Crystallogr D Biol Crystallogr. 2013 Sep;69(Pt 9):1864.

Abstract

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.

PMID:
11976508
[Indexed for MEDLINE]

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