Consists of a derived database merging information from three-dimensional structures and one-dimensional sequences of proteins. HSSP is a resource of aligned sequence families, but also a database of implied secondary and tertiary structures. It can be useful for analyzing residue conservation in structural context, for defining structurally meaningful sequence patterns and, in general, for studying protein evolution, folding and design.
Provides access to experimentally derived information about the human proteome including protein–protein interactions (PPIs), post-translational modifications (PTMs) and tissue expression. HPRD is an integrated knowledgebase for genomic and proteomic investigators. The database also includes (i) PhosphoMotif Finder that contains known kinase/phosphatase substrate and binding motifs, (ii) links to a signaling pathway resource called NetPath, (iii) a distributed annotation system, called Human Proteinpedia for enhanced community participation and allows the use of BLAST for querying mRNA/protein data.
The polyproline helix type II (PPII) is a regular protein secondary structure with remarkable features. Many studies have highlighted different crucial biological roles supported by this local conformation, e.g. in the interactions between biological macromolecules. Although PPII is less frequently present than regular secondary structures such as canonical alpha helices and beta strands, it corresponds to 3–10% of residues. Up to now, PPII is not assigned by most popular assignment tools, and therefore, remains insufficiently studied. PolyprOnline database is, therefore, dedicated to PPII structure assignment and analysis to facilitate the study of PPII structure and functional roles.
A free resource to provide high quality information of WD40 protein structures and hotspot residues. To better serve the community, a user-friendly interactive web interface to browse, search and download the secondary structures, 3D structure models and potential hotspot residues has been implemented.
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