iMOTdb--a comprehensive collection of spatially interacting motifs in proteins.

Ganesan Pugalenthi*, Anirban Bhaduri, R. Sowdhamini

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Realization of conserved residues that represent a protein family is crucial for clearer understanding of biological function as well as for the better recognition of additional members in sequence databases. Functionally important residues are recognized well due to their high degree of conservation in closely related sequences and are annotated in functional motif databases. Structural motifs are central to the integrity of the fold and require careful analysis for their identification. We report the availability of a database of spatially interacting motifs in single protein structures as well as those among distantly related protein structures that belong to a superfamily. Spatial interactions amongst conserved motifs are automatically measured using sequence similarity scores and distance calculations. Interactions between pairs of conserved motifs are described in the form of pseudoenergies. iMOTdb database provides information for 854,488 motifs corresponding to 60,849 protein structural domains and 22,648 protein structural entries.

Original languageEnglish (US)
Pages (from-to)D285-286
Issue numberDatabase issue
StatePublished - Jan 1 2006
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


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