Validation and correction of Zn-Cys<sub>x</sub>His<sub>y</sub> complexes.

Touw, Wouter G; van Beusekom, Bart; Evers, Jochem M G; Vriend, Gert; Joosten, Robbie P

Validation and correction of Zn-Cys_xHis_y complexes.

Touw, Wouter G; van Beusekom, Bart; Evers, Jochem M G; Vriend, Gert; Joosten, Robbie P.

Afiliación

Touw WG; Centre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
van Beusekom B; Department of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Evers JM; Centre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
Vriend G; Centre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
Joosten RP; Department of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.

Acta Crystallogr D Struct Biol ; 72(Pt 10): 1110-1118, 2016 10 01.

Article en En | MEDLINE | ID: mdl-27710932

RESUMEN

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.

Asunto(s)

Cisteína/química; Histidina/química; Proteínas/química; Zinc/química; Sitios de Unión; Complejos de Coordinación/química; Cristalografía por Rayos X; Bases de Datos de Proteínas; Ligandos; Modelos Moleculares; Conformación Proteica

Palabras clave

geometric restraints; protein zinc-binding site; refinement; validation; zinc metal-site geometry

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Zinc / Proteínas / Cisteína / Histidina Idioma: En Revista: Acta Crystallogr D Struct Biol Año: 2016 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos

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