Provides the hot region information of the interfaces by using predicted hot spot residues, and structural properties of these interface residues such as pair potentials of interface residues, accessible surface area (ASA) and relative ASA values of interface residues of both monomer and complex forms of proteins. Also, the 3D visualization of the interface and interactions among hot spot residues are provided.
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.
Provides a public repository of computationally annotated hot spots in protein complexes for which the 3D structure is known. PCRPi-DB provides information for drug discovery, structure-based protein design and can be also used in large-scale studies aimed at gaining further understanding on protein–protein interactions (PPIs). This resource is cross-linked to several major databases thus increasing the range of information offered to users.
Catalogs every protein-protein interaction whose structure is available in the Protein Data Bank and which exhibits one or more helices at the interface. HippDB accepts queries on variables such as helix length and sequence, and it provides computational alanine scanning and change in solvent-accessible surface area values for every interfacial residue. HippDB is intended to serve as a starting point for structure-based small molecule and peptidomimetic drug development.
Makes information about protein interactive function easily accessible. BID organizes the vast amount of protein interaction information into tables, graphical contact maps and descriptive functional profiles. It stores the characterization of protein–protein binding interfaces at the amino acid level, so that the data is easily accessible and searchable. The database contains 170 protein pairs and over 1300 mutations.