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CoDNaS / Conformational Diversity of Native State
A collection of redundant crystallographic structures for a given protein extensively linked with structural, biological and physicochemical information. CoDNaS offers a well curated database that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitates the extraction of key information on small structural differences based on protein movements. CoDNaS enables users to easily relate the degree of conformational diversity with physical, chemical and biological properties derived from experiments on protein structure and biological characteristics. The new version of CoDNaS includes ∼70% of all available protein structures, and new tools have been added that run sequence searches, display structural flexibility profiles and allow users to browse the database for different structural classes. These tools facilitate the exploration of protein conformational diversity and its role in protein function.
Provides comprehensive information and a sophisticated interface for exploring conformational changes in proteins and their possible causes. All information is visualized in a unified and well-aligned manner, which is critical for capturing the relevance of different biological features. Possible applications of CCProf include analyses of protein disorder, secondary structure transition, protein flexibility/plasticity, protein interaction, post-translational modification and molecular dynamics. The update script of CCProf is executed weekly. The CCProf contains 986 187 protein structure pairs for 3123 proteins. In addition, CCProf provides a 3D view in which users can see the protein structures before and after conformational changes as well as binding targets that induce conformational changes.
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