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THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

The structure was published by Raghunathan, S., Chandross, R.J., Cheng, B.P., Persechini, A., Sobottka, S.E., and Kretsinger, R.H., in 1993 in a paper entitled "The linker of des-Glu84-calmodulin is bent." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 1993.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CALMODULIN. This molecule has the UniProt identifier P62157 (CALM_BOVIN)search. The sample contained 142 residues which is 95% of the natural sequence. Out of 142 residues 19 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 (6-148) (CALM_BOVIN)search Bos taurussearch 95% 142 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62157 (6 - 148) CALMODULIN Bos taurus

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P62157) Calmodulin-likesearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

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

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