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- PDB-6bcy: Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T360 -
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Open data
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Basic information
Entry | Database: PDB / ID: 6bcy | ||||||
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Title | Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T360 | ||||||
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![]() | SIGNALING PROTEIN / phosphate binding protein / protein complex / cytoskeleton regulation / cell motility | ||||||
Function / homology | ![]() RHO GTPases activate PKNs / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / neuron projection branch point / dendritic spine cytoplasm / negative regulation of monoatomic ion transmembrane transport / plasma membrane organization / TP53 Regulates Metabolic Genes / actin crosslink formation ...RHO GTPases activate PKNs / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / neuron projection branch point / dendritic spine cytoplasm / negative regulation of monoatomic ion transmembrane transport / plasma membrane organization / TP53 Regulates Metabolic Genes / actin crosslink formation / positive regulation of dendritic spine morphogenesis / cellular response to L-glutamate / protein localization to synapse / cadherin binding involved in cell-cell adhesion / cytoskeletal anchor activity / regulation of modification of postsynaptic actin cytoskeleton / presynaptic cytosol / neuron projection terminus / proline-rich region binding / postsynaptic cytosol / small GTPase-mediated signal transduction / positive regulation of actin filament polymerization / dendrite development / positive regulation of excitatory postsynaptic potential / actin filament bundle assembly / CDC42 GTPase cycle / Regulation of localization of FOXO transcription factors / excitatory synapse / Activation of BAD and translocation to mitochondria / RHO GTPases Activate WASPs and WAVEs / RAC3 GTPase cycle / postsynaptic density, intracellular component / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / cellular response to epidermal growth factor stimulus / 14-3-3 protein binding / ruffle / RAC1 GTPase cycle / substantia nigra development / axonogenesis / dendritic shaft / synaptic membrane / secretory granule / filopodium / transcription coregulator binding / PDZ domain binding / Translocation of SLC2A4 (GLUT4) to the plasma membrane / regulation of actin cytoskeleton organization / TP53 Regulates Metabolic Genes / adherens junction / FCGR3A-mediated phagocytosis / Schaffer collateral - CA1 synapse / regulation of synaptic plasticity / protein localization / Regulation of actin dynamics for phagocytic cup formation / VEGFA-VEGFR2 Pathway / lamellipodium / insulin receptor signaling pathway / regulation of cell shape / scaffold protein binding / microtubule / transmembrane transporter binding / protein domain specific binding / focal adhesion / negative regulation of DNA-templated transcription / neuronal cell body / glutamatergic synapse / synapse / signal transduction / protein-containing complex / extracellular exosome / nucleoplasm / identical protein binding / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Kast, D.J. / Dominguez, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanism of IRSp53 inhibition by 14-3-3. Authors: Kast, D.J. / Dominguez, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 571.5 KB | Display | ![]() |
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PDB format | ![]() | 484.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 789.3 KB | Display | ![]() |
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Full document | ![]() | 800.6 KB | Display | |
Data in XML | ![]() | 35.6 KB | Display | |
Data in CIF | ![]() | 47.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6bcrC ![]() 6bd1C ![]() 6bd2C ![]() 6bqtC ![]() 2br9S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein / Protein/peptide , 2 types, 8 molecules ABEFCDGH
#1: Protein | Mass: 27795.234 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1473.481 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) ![]() |
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-Non-polymers , 6 types, 120 molecules ![](data/chem/img/PEG.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PG4.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PG4.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | #7: Chemical | ChemComp-PE4 / | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.67 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.1M Magnesium Formate, 13% Peg 3350, 4% 2,2,2-Trifluoroethanol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 23, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9769 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→21.847 Å / Num. obs: 49462 / % possible obs: 96.6 % / Redundancy: 3.6 % / Biso Wilson estimate: 35.77 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.087 / Net I/σ(I): 12.5 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.579 / Mean I/σ(I) obs: 3.6 / Num. unique obs: 4819 / CC1/2: 0.87 / % possible all: 94.3 |
-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2BR9 Resolution: 2.3→21.847 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 25.98
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 213.31 Å2 / Biso mean: 59.3296 Å2 / Biso min: 19.13 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.3→21.847 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14
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