Database of protein conformational diversity

{{infobox biodatabase

|title = PCDB

|logo =File:Database.png

|description = Protein conformational diversity.

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|center =Universidad Nacional de Quilmes

|laboratory = Centro de Estudios e Investigaciones

|author = Ezequiel I Juritz

|citation = Juritz & al. (2011)

|released = 2010

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|url = http://www.pcdb.unq.edu.ar

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The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography.{{cite journal |vauthors=Juritz EI, Alberti SF, Parisi GD | title = PCDB: a database of protein conformational diversity | journal = Nucleic Acids Res. | volume = 39 | issue = Database issue | pages = D475–9 |date=January 2011 | pmid = 21097895 | pmc = 3013735 | doi = 10.1093/nar/gkq1181 }}{{cite journal |vauthors=Galperin MY, Cochrane GR | title = The 2011 Nucleic Acids Research Database Issue and the online Molecular Biology Database Collection | journal = Nucleic Acids Res. | volume = 39 | issue = Database issue | pages = D1–6 |date=January 2011 | pmid = 21177655 | pmc = 3013748 | doi = 10.1093/nar/gkq1243 }} Proteins are inherently flexible and this database collects information on this subject for use in molecular research. It uses the CATH database as a source of structures for each protein and reports the range of differences in the structures based on their superposition and reports a maximum RMSD. The interface for the database allows researchers to find proteins with a range of conformational flexibility allowing them to find highly flexible proteins for example. The database is run and maintained by a group of researchers based at the Universidad Nacional de Quilmes in Argentina.{{cn|date=November 2023}}