Provides unbiased training and validation datasets for the development of algorithms to predict binding affinity changes due to missense mutations. The PROXiMATE database helps about the study of disease-causing mutations in the progression, diagnosis and treatment of various diseases. It gives possible drug targets and novel therapy options. More, it supplies experimental data for the identification of mutants which show increased affinity to their interacting partners.
Informs about structural effects of variations of the enzyme galactose-1-phosphate uridylyltransferase (GALT), Galactosemia, or genetic disease. The GALT protein database is an online resource that allows researchers to access results of several types of protein surveys. One of its objectives is to allow a more in-depth study of the structural and functional effects of variations on proteins.
Studies the impacts of missense mutations on the interaction of ligands with the proteome. This manually curated, literature-derived database, comprising over 1000 mutations, associates for the first time experimental information on changes in affinity with three-dimensional structures of protein-ligand complexes.
A database encompassing comprehensive annotations for all genes having ligand binding site mutations. mutLBSgeneDB may contribute to systematic analysis for functional annotations of genes with ligand binding site mutations for cancer and drug research in the precision medicine era. mutLBSgeneDB collected and curated over 2300 genes (mutLBSgenes) having around 12 000 somatic mutations at around 10 000 LBSs across 16 cancer types and selected 744 drug targetable genes (targetable_mutLBSgenes) by incorporating kinases, transcription factors, pharmacological genes, and cancer driver genes.
A database that provides access to various structural data sets and integrated functionalities not yet available to the community. The originality of the SPROUTS database is the ability to gain access to a variety of structural analyses at one place and with a strong interaction between them. SPROUTS combines data pertaining to 429 structures that capture representative folds and results related to the prediction of critical residues expected to belong to the folding nucleus: the MIR (Most Interacting Residues), the description of the structures in terms of modular fragments: the TEF (Tightened End Fragments), and the calculation at each position of the free energy change gradient upon mutation by one of the 19 amino acids. All database results can be displayed and downloaded in textual files and Excel spreadsheets and visualized on the protein structure. SPROUTS is a unique resource to access as well as visualize state-of-the-art characteristics of protein folding and analyse the effect of point mutations on protein structure.
Allows to search single alanine mutations in protein–protein, protein–nucleic acid, and protein–small molecule interactions for which binding affinities have been experimentally determined. ASEdb contains surface areas of the mutated side chain and links to the PDB entries. It is useful for studying the contribution of single amino acids to the energetics of protein interactions, and can be updated by researchers as new data are generated.
Provides full annotation of missense variants of all human proteins with multi-level characterization including details of the physico-chemical changes induced by the amino acid modification, information related to the conservation of the mutated residue and its position relative to functional features in available or calculated 3D model. The major release of the MSV3d database is generated and updated regularly according to the dbSNP 137 (database of Single Nucleotide Polymorphism) and SwissVar releases.
Allows users to detect similar energy profiles, relevant structural and functional relationships. ePRoS is a database for energy profile-based studying and comparing sequence–structure–function relationships and protein stability. It stores more than 74 000 pre-calculated energy profiles derived from experimental globular protein structures and about 1300 pre-calculated profiles of a-helical membrane protein structures. It offers users different way to visualize, download, and access energy profile data.
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