+Open data
-Basic information
Entry | Database: PDB / ID: 4gnt | ||||||
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Title | Complex of ChREBP and 14-3-3beta | ||||||
Components |
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Keywords | PROTEIN BINDING / protein-protein complex / alpha-alpha helical / protein-protein interaction / 14-3-3 / cytoplasm/nucleus | ||||||
Function / homology | Function and homology information : / : / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / carbohydrate response element binding / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Regulation of localization of FOXO transcription factors / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / RHO GTPases activate PKNs / regulation of cell cycle => GO:0051726 / Activation of BAD and translocation to mitochondria ...: / : / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / carbohydrate response element binding / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Regulation of localization of FOXO transcription factors / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / RHO GTPases activate PKNs / regulation of cell cycle => GO:0051726 / Activation of BAD and translocation to mitochondria / Frs2-mediated activation / MTOR signalling / Signaling by Hippo / Negative regulation of MAPK pathway / negative regulation of protein dephosphorylation / glucose mediated signaling pathway / TP53 Regulates Metabolic Genes / RAF activation / mTORC1-mediated signalling / MAP2K and MAPK activation / Rap1 signalling / cytoplasmic sequestering of protein / negative regulation of G protein-coupled receptor signaling pathway / positive regulation of fatty acid biosynthetic process / negative regulation of oxidative phosphorylation / regulation of glycolytic process / protein kinase inhibitor activity / transcription factor binding / phosphoserine residue binding / protein targeting / response to glucose / fatty acid homeostasis / energy homeostasis / negative regulation of peptidyl-serine phosphorylation / positive regulation of lipid biosynthetic process / transcription repressor complex / positive regulation of glycolytic process / cellular response to glucose stimulus / phosphoprotein binding / intracellular protein transport / DNA-binding transcription repressor activity, RNA polymerase II-specific / histone deacetylase binding / melanosome / glucose homeostasis / transcription regulator complex / sequence-specific DNA binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / protein heterodimerization activity / protein domain specific binding / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / protein-containing complex binding / regulation of transcription by RNA polymerase II / protein kinase binding / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.41 Å | ||||||
Authors | Zhang, H. / Huang, N. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of Carbohydrate Response Element Binding Protein (ChREBP) in complex with 14-3-3b Authors: Ge, Q. / Huang, N. / Zhang, H. / Uyeda, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4gnt.cif.gz | 120 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4gnt.ent.gz | 95.2 KB | Display | PDB format |
PDBx/mmJSON format | 4gnt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gn/4gnt ftp://data.pdbj.org/pub/pdb/validation_reports/gn/4gnt | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 28240.658 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ywhab / Production host: Escherichia coli (E. coli) / References: UniProt: Q9CQV8 | ||
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#2: Protein/peptide | Mass: 2768.206 Da / Num. of mol.: 1 / Fragment: UNP residues 117-137 / Source method: obtained synthetically / Source: (synth.) Mus musculus (house mouse) / References: UniProt: Q99MZ3 | ||
#3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.8 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM sodium citrate, 200mM sodium/potassium tartrate, 2.2M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1 Å |
Detector | Date: Mar 1, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.41→33.7 Å / Num. all: 29835 / Num. obs: 28628 / % possible obs: 3.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.41→33.74 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.931 / SU B: 15.335 / SU ML: 0.158 / Cross valid method: THROUGHOUT / ESU R: 0.297 / ESU R Free: 0.229 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 84.541 Å2
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Refinement step | Cycle: LAST / Resolution: 2.41→33.74 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.411→2.474 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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