Validation and correction of Zn-Cys_xHis_y complexes.

ABSTRACT: 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.

SUBMITTER: Touw WG 

PROVIDER: S-EPMC5053137 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature