2r28 Summary

pdbe.org/2r28
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The complex Structure of Calmodulin Bound to a Calcineurin Peptide

The structure was published by Ye, Q., Wang, H., Zheng, J., Wei, Q., and Jia, Z., in 2008 in a paper entitled "The complex structure of calmodulin bound to a calcineurin peptide." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.86 Å and deposited in 2007.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Calmodulin and Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform.

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 heterotetramers.

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 P62158 (1-149) (CALM_HUMAN)search Homo sapienssearch 97% 149 96%
B Calmodulin P62158 (1-149) (CALM_HUMAN)search Homo sapienssearch 97% 149 96%
C Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Q08209 (389-413) (PP2BA_HUMAN)search Homo sapienssearch 100% 25 76%
D Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Not available
Homo sapienssearch < 90% 25 76%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P62158 (1 - 149) Calmodulin Homo sapiens
Q08209 (389 - 413) Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A, B (P62158) Calmodulin-likesearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch
C, D (Q08209)

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P62158) calcium ion bindingsearch protein bindingsearch nitric-oxide synthase regulator activitysearch ion channel bindingsearch metal ion bindingsearch protein domain specific bindingsearch thioesterase bindingsearch protein kinase bindingsearch protein N-terminus bindingsearch type 3 metabotropic glutamate receptor bindingsearch calcium-dependent protein bindingsearch enzyme regulator activitysearch protein serine/threonine kinase activator activitysearch titin bindingsearch phospholipase bindingsearch phosphatidylinositol 3-kinase bindingsearch adenylate cyclase bindingsearch N-terminal myristoylation domain bindingsearch nitric-oxide synthase bindingsearch protein phosphatase activator activitysearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch glucose metabolic processsearch epidermal growth factor receptor signaling pathwaysearch positive regulation of cyclic nucleotide metabolic processsearch positive regulation of protein dephosphorylationsearch blood coagulationsearch innate immune responsesearch rhodopsin mediated signaling pathwaysearch regulation of high voltage-gated calcium channel activitysearch activation of phospholipase C activitysearch glycogen catabolic processsearch platelet degranulationsearch inositol phosphate metabolic processsearch small molecule metabolic processsearch Fc-epsilon receptor signaling pathwaysearch positive regulation of protein serine/threonine kinase activitysearch fibroblast growth factor receptor signaling pathwaysearch regulation of nitric-oxide synthase activitysearch synaptic transmissionsearch regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ionsearch regulation of cytokinesissearch positive regulation of phosphoprotein phosphatase activitysearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of peptidyl-threonine phosphorylationsearch substantia nigra developmentsearch detection of calcium ionsearch carbohydrate metabolic processsearch phototransduction, visible lightsearch platelet activationsearch nitric oxide metabolic processsearch activation of adenylate cyclase activitysearch positive regulation of cyclic-nucleotide phosphodiesterase activitysearch negative regulation of peptidyl-threonine phosphorylationsearch signal transductionsearch regulation of ryanodine-sensitive calcium-release channel activitysearch neurotrophin TRK receptor signaling pathwaysearch response to amphetaminesearch positive regulation of protein autophosphorylationsearch regulation of heart ratesearch response to corticosteronesearch response to calcium ionsearch muscle contractionsearch regulation of cardiac muscle contractionsearch regulation of cell communication by electrical coupling involved in cardiac conductionsearch G-protein coupled receptor signaling pathwaysearch regulation of rhodopsin mediated signaling pathwaysearch calcium-mediated signalingsearch positive regulation of nitric-oxide synthase activitysearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch membrane organizationsearch neuron projectionsearch cytosolsearch nucleoplasmsearch sarcomeresearch plasma membranesearch cytoplasmsearch extracellular regionsearch extracellular vesicular exosomesearch spindle microtubulesearch spindlesearch spindle polesearch nucleussearch centrosomesearch cytoskeletonsearch vesiclesearch growth conesearch calcium channel complexsearch

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