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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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
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author Touw, Wouter G.
van Beusekom, Bart
Evers, Jochem M. G.
Vriend, Gert
Joosten, Robbie P.
author_facet Touw, Wouter G.
van Beusekom, Bart
Evers, Jochem M. G.
Vriend, Gert
Joosten, Robbie P.
author_sort Touw, Wouter G.
collection PubMed
description 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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spelling pubmed-50531372016-10-13 Validation and correction of Zn–Cys(x)His(y) complexes Touw, Wouter G. van Beusekom, Bart Evers, Jochem M. G. Vriend, Gert Joosten, Robbie P. Acta Crystallogr D Struct Biol Research Papers 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. International Union of Crystallography 2016-09-15 /pmc/articles/PMC5053137/ /pubmed/27710932 http://dx.doi.org/10.1107/S2059798316013036 Text en © Touw et al. 2016 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Papers
Touw, Wouter G.
van Beusekom, Bart
Evers, Jochem M. G.
Vriend, Gert
Joosten, Robbie P.
Validation and correction of Zn–Cys(x)His(y) complexes
title Validation and correction of Zn–Cys(x)His(y) complexes
title_full Validation and correction of Zn–Cys(x)His(y) complexes
title_fullStr Validation and correction of Zn–Cys(x)His(y) complexes
title_full_unstemmed Validation and correction of Zn–Cys(x)His(y) complexes
title_short Validation and correction of Zn–Cys(x)His(y) complexes
title_sort validation and correction of zn–cys(x)his(y) complexes
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053137/
https://www.ncbi.nlm.nih.gov/pubmed/27710932
http://dx.doi.org/10.1107/S2059798316013036
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