PIBASE: a comprehensive database of structurally defined protein interfaces. Motivation: In recent years, the Protein Data Bank (PDB) has experienced rapid growth. To maximize the utility of the high resolution protein–protein interaction data stored in the PDB, we have developed PIBASE, a comprehensive relational database of structurally defined interfaces between pairs of protein domains. It is composed of binary interfaces extracted from structures in the PDB and the Probable Quaternary Structure server using domain assignments from the Structural Classification of Proteins and CATH fold classification systems. Results: PIBASE currently contains 158 915 interacting domain pairs between 105 061 domains from 2125 SCOP families. A diverse set of geometric, physiochemical and topologic properties are calculated for each complex, its domains, interfaces and binding sites. A subset of the interface properties are used to remove interface redundancy within PDB entries, resulting in 20 912 distinct domain–domain interfaces. The complexes are grouped into 989 topological classes based on their patterns of domain–domain contacts. The binary interfaces and their corresponding binding sites are categorized into 18 755 and 30 975 topological classes, respectively, based on the topology of secondary structure elements. The utility of the database is illustrated by outlining several current applications. Availability: The database is accessible via the world wide web at http://salilab.org/pibase

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  1. von Stechow, Louise (ed.); Delgado, Alberto Santos (ed.): Computational cell biology. Methods and protocols (2018)
  2. Teyra, Joan; Paszkowski-Rogacz, Maciej; Anders, Gerd; Pisabarro, M. Teresa: SCOWLP classification: Structural comparison and analysis of protein binding regions (2008) ioport