2o5g Summary

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Calmodulin-smooth muscle light chain kinase peptide complex

A publication describing this structure is not available. The depositing authors are Valentine, K.G.search; Ng, H.L.search; Schneeweis, J.K.search; Kranz, J.K.search; Frederick, K.K.search; Alber, T.search; Wand, A.J.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.08 Å and deposited in 2006.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Calmodulin and Smooth muscle Myosin light chain kinase peptide.

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 most likely forms heterodimers.

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 P62149 (2-149) (CALM_CHICK)search Gallus gallussearch 98% 148 99%
B Smooth muscle Myosin light chain kinase peptide P11799 (1730-1748) (MYLK_CHICK)search Gallus gallussearch < 90% 21 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P62149 (2 - 149) Calmodulin Gallus gallus
P11799 (1730 - 1748) Smooth muscle Myosin light chain kinase peptide

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P62149) Calmodulin-likesearch PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch
B

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P62149) calcium ion bindingsearch phospholipase bindingsearch protein domain specific bindingsearch titin bindingsearch protein phosphatase activator activitysearch thioesterase bindingsearch N-terminal myristoylation domain bindingsearch ion channel bindingsearch myosin bindingsearch metal ion bindingsearch regulation of cardiac muscle contractionsearch positive regulation of cyclic nucleotide metabolic processsearch regulation of heart ratesearch positive regulation of protein dephosphorylationsearch detection of calcium ionsearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of cyclic-nucleotide phosphodiesterase activitysearch response to calcium ionsearch regulation of cytokinesissearch positive regulation of phosphoprotein phosphatase activitysearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch spindle polesearch calcium channel complexsearch spindle microtubulesearch centrosomesearch sarcomeresearch

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