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On their surface, proteins are shaped into numerous depressions and protrusions that provide unique microenvironments for ligand binding and catalysis. The dynamics, size and chemical properties of these cavities are essential for a mechanistic understanding of protein function. Here, we present CaviDB, a novel database of cavities and their features in known protein structures. It integrates the results of commonly used cavity detection software with protein features derived from sequence, structural and functional analyses. Each protein in CaviDB is linked to its corresponding conformers, which also facilitates the study of conformational changes in cavities. Our initial release includes \u223c927\u2009773 distinct proteins, as well as the characterization of 36\u2009136\u2009869 cavities, of which 1\u2009147\u2009034 were predicted to be drug targets. The structural focus of CaviDB provides the ability to compare cavities and their properties from different conformational states of the protein. CaviDB not only aims to provide a comprehensive database that can be used for various aspects of drug design and discovery but also contributes to a better understanding of the fundamentals of protein structure\u2013function relationships. With its unique approach, CaviDB represents an indispensable resource for the large community of bioinformaticians in particular and biologists in general.<\/jats:p><jats:p>Database URL https:\/\/www.cavidb.org<\/jats:p>","DOI":"10.1093\/database\/baad010","type":"journal-article","created":{"date-parts":[[2023,5,11]],"date-time":"2023-05-11T06:52:32Z","timestamp":1683787952000},"source":"Crossref","is-referenced-by-count":7,"title":["CaviDB: a database of cavities and their features in the structural and conformational space of proteins"],"prefix":"10.1093","volume":"2023","author":[{"given":"Ana Julia","family":"Velez Rueda","sequence":"first","affiliation":[{"name":"Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes , Roque Saenz Pena 182, Bernal B1876BXD, Argentina"}]},{"given":"Franco Leonardo","family":"Bulgarelli","sequence":"additional","affiliation":[{"name":"Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes , Roque Saenz Pena 182, Bernal B1876BXD, Argentina"}]},{"given":"Nicol\u00e1s","family":"Palopoli","sequence":"additional","affiliation":[{"name":"Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes , Roque Saenz Pena 182, Bernal B1876BXD, Argentina"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7444-1624","authenticated-orcid":false,"given":"Gustavo","family":"Parisi","sequence":"additional","affiliation":[{"name":"Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes , Roque Saenz Pena 182, Bernal B1876BXD, Argentina"}]}],"member":"286","published-online":{"date-parts":[[2023,5,10]]},"reference":[{"key":"2023051013580834000_R1","doi-asserted-by":"crossref","first-page":"22146","DOI":"10.1073\/pnas.1917770117","article-title":"Structural cavities are critical to balancing stability and activity of a membrane-integral enzyme","volume":"117","author":"Guo","year":"2020","journal-title":"Proc. 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