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Open data
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Basic information
Entry | Database: PDB / ID: 1ckk | ||||||
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Title | CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT | ||||||
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![]() | CALMODULIN-PEPTIDE COMPLEX / COMPLEX (CALMODULIN-PEPTIDE) / CALMODULIN / CAMKK | ||||||
Function / homology | ![]() CaMK IV-mediated phosphorylation of CREB / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of RAC1 downstream of NMDARs / protein serine/threonine kinase activity => GO:0004674 / Ca2+/calmodulin-dependent protein kinase / calcium/calmodulin-dependent protein kinase activity / activation of protein kinase activity / positive regulation of protein kinase activity / enzyme regulator activity / calmodulin binding ...CaMK IV-mediated phosphorylation of CREB / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of RAC1 downstream of NMDARs / protein serine/threonine kinase activity => GO:0004674 / Ca2+/calmodulin-dependent protein kinase / calcium/calmodulin-dependent protein kinase activity / activation of protein kinase activity / positive regulation of protein kinase activity / enzyme regulator activity / calmodulin binding / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / signaling receptor binding / protein serine/threonine kinase activity / calcium ion binding / nucleoplasm / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Osawa, M. / Tokumitsu, H. / Swindells, M.B. / Kurihara, H. / Orita, M. / Shibanuma, T. / Furuya, T. / Ikura, M. | ||||||
![]() | ![]() Title: A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase. Authors: Osawa, M. / Tokumitsu, H. / Swindells, M.B. / Kurihara, H. / Orita, M. / Shibanuma, T. / Furuya, T. / Ikura, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.6 MB | Display | ![]() |
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PDB format | ![]() | 1.3 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 360.9 KB | Display | ![]() |
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Full document | ![]() | 910.1 KB | Display | |
Data in XML | ![]() | 135.9 KB | Display | |
Data in CIF | ![]() | 181.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 16721.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 3023.702 Da / Num. of mol.: 1 / Fragment: CALMODULIN BINDING DOMAIN Source method: isolated from a genetically manipulated source Details: 26-RESIDUE SYNTHETIC PEPTIDE / Source: (gene. exp.) ![]() ![]() References: UniProt: P97756, Ca2+/calmodulin-dependent protein kinase |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | Ionic strength: 100mM KCL, 10mM CACL2 / pH: 6.7 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 30 |