+Open data
-Basic information
Entry | Database: PDB / ID: 7cqp | |||||||||
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Title | Complex of TRPC4 and Calmodulin_Nlobe | |||||||||
Components |
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Keywords | SIGNALING PROTEIN / Calmodulin / TRP channel | |||||||||
Function / homology | Function and homology information regulation of action potential firing rate / positive regulation of store-operated calcium entry / CaMK IV-mediated phosphorylation of CREB / Cam-PDE 1 activation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Glycogen breakdown (glycogenolysis) / Activation of RAC1 downstream of NMDARs / Reduction of cytosolic Ca++ levels / Sodium/Calcium exchangers / Activation of Ca-permeable Kainate Receptor ...regulation of action potential firing rate / positive regulation of store-operated calcium entry / CaMK IV-mediated phosphorylation of CREB / Cam-PDE 1 activation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Glycogen breakdown (glycogenolysis) / Activation of RAC1 downstream of NMDARs / Reduction of cytosolic Ca++ levels / Sodium/Calcium exchangers / Activation of Ca-permeable Kainate Receptor / CLEC7A (Dectin-1) induces NFAT activation / Synthesis of IP3 and IP4 in the cytosol / RHO GTPases activate PAKs / Calmodulin induced events / Inactivation, recovery and regulation of the phototransduction cascade / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Calcineurin activates NFAT / eNOS activation / Ion transport by P-type ATPases / presynaptic endocytosis / Unblocking of NMDA receptors, glutamate binding and activation / Protein methylation / RAF activation / VEGFR2 mediated vascular permeability / RAS processing / Smooth Muscle Contraction / Ca2+ pathway / gamma-aminobutyric acid secretion / FCERI mediated Ca+2 mobilization / RHO GTPases activate IQGAPs / Extra-nuclear estrogen signaling / RAF/MAP kinase cascade / store-operated calcium channel activity / PKA activation / Platelet degranulation / cation channel complex / TRP channels / Stimuli-sensing channels / Ion homeostasis / type 3 metabotropic glutamate receptor binding / inositol 1,4,5 trisphosphate binding / calcium ion import / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / regulation of cardiac muscle cell action potential / cortical cytoskeleton / nitric-oxide synthase binding / oligodendrocyte differentiation / negative regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / regulation of calcium ion transport / calyx of Held / adenylate cyclase binding / catalytic complex / detection of calcium ion / regulation of cardiac muscle contraction / regulation of ryanodine-sensitive calcium-release channel activity / cellular response to interferon-beta / calcium channel inhibitor activity / phosphatidylinositol 3-kinase binding / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / : / titin binding / voltage-gated potassium channel complex / sperm midpiece / regulation of cytosolic calcium ion concentration / calcium channel complex / adenylate cyclase activator activity / nitric-oxide synthase regulator activity / regulation of heart rate / sarcomere / protein serine/threonine kinase activator activity / regulation of cytokinesis / caveola / spindle microtubule / calcium ion transmembrane transport / positive regulation of receptor signaling pathway via JAK-STAT / calcium channel activity / cellular response to type II interferon / G2/M transition of mitotic cell cycle / spindle pole / beta-catenin binding / calcium-dependent protein binding / calcium ion transport / cell-cell junction / myelin sheath / basolateral plasma membrane / growth cone / transmembrane transporter binding / cadherin binding / membrane raft / protein domain specific binding / centrosome / calcium ion binding / protein kinase binding / cell surface / protein-containing complex / nucleoplasm / plasma membrane Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å | |||||||||
Authors | Shen, Z.S. | |||||||||
Funding support | China, 2items
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Citation | Journal: Structure / Year: 2021 Title: Calmodulin binds to Drosophila TRP with an unexpected mode. Authors: Chen, W. / Shen, Z. / Asteriti, S. / Chen, Z. / Ye, F. / Sun, Z. / Wan, J. / Montell, C. / Hardie, R.C. / Liu, W. / Zhang, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7cqp.cif.gz | 34.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7cqp.ent.gz | 20.5 KB | Display | PDB format |
PDBx/mmJSON format | 7cqp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7cqp_validation.pdf.gz | 421.9 KB | Display | wwPDB validaton report |
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Full document | 7cqp_full_validation.pdf.gz | 423.1 KB | Display | |
Data in XML | 7cqp_validation.xml.gz | 6 KB | Display | |
Data in CIF | 7cqp_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cq/7cqp ftp://data.pdbj.org/pub/pdb/validation_reports/cq/7cqp | HTTPS FTP |
-Related structure data
Related structure data | 7cqhC 7cqvC 1up5S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 8868.894 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Calm1, Calm, Cam, Cam1 / Production host: Escherichia coli (E. coli) / References: UniProt: P0DP26 | ||||
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#2: Protein/peptide | Mass: 3365.822 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse) / References: UniProt: Q9QUQ5 | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.44 % |
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Crystal grow | Temperature: 289 K / Method: evaporation Details: 55.7% w/v Polyethylene glycol 1000, 150mM MES, 2% v/v 2-Methyl-2,4-pentanediol, pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9789 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 10, 2019 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.9→50 Å / Num. obs: 12754 / % possible obs: 99.7 % / Redundancy: 7.4 % / Rmerge(I) obs: 0.102 / Rpim(I) all: 0.039 / Rrim(I) all: 0.11 / Χ2: 0.938 / Net I/σ(I): 5.6 / Num. measured all: 330733 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1up5 Resolution: 1.9→40.988 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.7 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 54.34 Å2 / Biso mean: 27.54 Å2 / Biso min: 16.17 Å2 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.9→40.988 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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