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- PDB-6ctb: Apo-Calmodulin Bound to Calcium Voltage Gated Channel 1.2 IQ-Motif -
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Open data
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Basic information
Entry | Database: PDB / ID: 6ctb | ||||||
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Title | Apo-Calmodulin Bound to Calcium Voltage Gated Channel 1.2 IQ-Motif | ||||||
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![]() | PROTEIN BINDING / calmodulin / surface expression / Cav1.2 / apo-calmodulin / voltage gated channel / calcium / neuronal signaling | ||||||
Function / homology | ![]() regulation of membrane repolarization during action potential / calcium ion transmembrane transport via high voltage-gated calcium channel / positive regulation of adenylate cyclase activity / high voltage-gated calcium channel activity / cardiac conduction / L-type voltage-gated calcium channel complex / calcium ion transport into cytosol / voltage-gated calcium channel complex / voltage-gated calcium channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion ...regulation of membrane repolarization during action potential / calcium ion transmembrane transport via high voltage-gated calcium channel / positive regulation of adenylate cyclase activity / high voltage-gated calcium channel activity / cardiac conduction / L-type voltage-gated calcium channel complex / calcium ion transport into cytosol / voltage-gated calcium channel complex / voltage-gated calcium channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / enzyme regulator activity / T-tubule / calcium ion transmembrane transport / postsynaptic density membrane / sarcolemma / positive regulation of cytosolic calcium ion concentration / perikaryon / postsynaptic density / calmodulin binding / signaling receptor binding / calcium ion binding / dendrite / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Turner, M.L. / Anderson, D.E. / Ames, J.B. | ||||||
Funding support | ![]()
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![]() | ![]() Title: apo-Calmodulin Bound to Calcium Voltage Gated Channel 1.2 IQ-Motif Authors: Turner, M.L. / Anderson, D.E. / Ames, J.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.2 KB | Display | ![]() |
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PDB format | ![]() | 99.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 805.1 KB | Display | ![]() |
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Full document | ![]() | 845.1 KB | Display | |
Data in XML | ![]() | 29.8 KB | Display | |
Data in CIF | ![]() | 40.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16650.273 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: pBR322 based IG-lambda expression vector (others) References: UniProt: P0DP33 |
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#2: Protein/peptide | Mass: 3120.665 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: pBR322 based IG-lambda expression vector (others) References: UniProt: P15381 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Details: 20mM Potassium Phosphate pH 6.0, 100mM KCl, 1mM EDTA-d12 Ionic strength: 100 mM / Label: conditions 1 / pH: 6 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 600 MHz / Details: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 2 / Details: used with all structures along with rigid docking | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: l / Conformers calculated total number: 200 / Conformers submitted total number: 4 |