Validation and correction of Zn–Cys(x)His(y) complexes

Many crystal structures in the Protein Data Bank contain zinc ions in a geometrically distorted tetrahedral complex with four Cys and/or His ligands. A method is presented to automatically validate and correct these zinc complexes. Analysis of the corrected zinc complexes shows that the average Zn–C...

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Detalles Bibliográficos
Autores principales: Touw, Wouter G., van Beusekom, Bart, Evers, Jochem M. G., Vriend, Gert, Joosten, Robbie P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2016
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053137/
https://www.ncbi.nlm.nih.gov/pubmed/27710932
http://dx.doi.org/10.1107/S2059798316013036
Descripción
Sumario:Many crystal structures in the Protein Data Bank contain zinc ions in a geometrically distorted tetrahedral complex with four Cys and/or His ligands. A method is presented to automatically validate and correct these zinc complexes. Analysis of the corrected zinc complexes shows that the average Zn–Cys distances and Cys–Zn–Cys angles are a function of the number of cysteines and histidines involved. The observed trends can be used to develop more context-sensitive targets for model validation and refinement.

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