1prw Summary

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Crystal structure of bovine brain Ca++ calmodulin in a compact form

The structure was published by Fallon, J.L. and Quiocho, F.A., in 2003 in a paper entitled "A closed compact structure of native ca(2+)-calmodulin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Calmodulin. This molecule has the UniProt identifier P62157 (CALM_BOVIN)search. The sample contained 149 residues which is 99% of the natural sequence. Out of 149 residues 149 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Calmodulin P62157 (2-149) (CALM_BOVIN)search Bos taurussearch 95% 149 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62157 (2 - 149) Calmodulin Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62157) Calmodulin-likesearch EF-handsearch PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P62157) protein bindingsearch phospholipase bindingsearch thioesterase bindingsearch N-terminal myristoylation domain bindingsearch metal ion bindingsearch ion channel bindingsearch protein domain specific bindingsearch titin bindingsearch protein phosphatase activator activitysearch calcium ion bindingsearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch positive regulation of cyclic-nucleotide phosphodiesterase activitysearch regulation of heart ratesearch regulation of cardiac muscle contractionsearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of cyclic nucleotide metabolic processsearch positive regulation of phosphoprotein phosphatase activitysearch positive regulation of protein dephosphorylationsearch regulation of cytokinesissearch response to calcium ionsearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch detection of calcium ionsearch spindle polesearch spindlesearch centrosomesearch sarcomeresearch cytosolsearch spindle microtubulesearch cytoskeletonsearch cytoplasmsearch calcium channel complexsearch

Chain InterPro annotation
A EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch