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Yorodumi- PDB-5wfx: Structural basis for the interaction of 14-3-3beta with Tricarbox... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5wfx | ||||||
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Title | Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle intermediate Malate | ||||||
Components | 14-3-3 protein beta/alpha | ||||||
Keywords | PROTEIN TRANSPORT / ChREBP / transcription activation | ||||||
Function / homology | Function and homology information Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / 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 / Activation of BAD and translocation to mitochondria / Frs2-mediated activation / MTOR signalling / Signaling by Hippo / Negative regulation of MAPK pathway ...Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / 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 / Activation of BAD and translocation to mitochondria / Frs2-mediated activation / MTOR signalling / Signaling by Hippo / Negative regulation of MAPK pathway / TP53 Regulates Metabolic Genes / RAF activation / mTORC1-mediated signalling / negative regulation of protein dephosphorylation / MAP2K and MAPK activation / cytoplasmic sequestering of protein / Rap1 signalling / negative regulation of G protein-coupled receptor signaling pathway / protein kinase inhibitor activity / phosphoserine residue binding / protein targeting / transcription repressor complex / phosphoprotein binding / intracellular protein transport / histone deacetylase binding / melanosome / protein domain specific binding / negative regulation of DNA-templated transcription / protein-containing complex binding / perinuclear region of cytoplasm / enzyme binding / signal transduction / protein-containing complex / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.651 Å | ||||||
Authors | Hou, Z.Q. | ||||||
Citation | Journal: To Be Published Title: Structural basis for the interaction of 14-3-3 beta withTricarboxylic Acid Cycle intermediate Malate Authors: Hou, Z.Q. / Su, L.J. / Liu, X.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5wfx.cif.gz | 118.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5wfx.ent.gz | 90.6 KB | Display | PDB format |
PDBx/mmJSON format | 5wfx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/5wfx ftp://data.pdbj.org/pub/pdb/validation_reports/wf/5wfx | HTTPS FTP |
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-Related structure data
Related structure data | 5wfuS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 28118.404 Da / Num. of mol.: 2 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 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.6 % |
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Crystal grow | Temperature: 291 K / Method: evaporation / pH: 7 / Details: 2.2M Sodium Malonate pH7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97929 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 17, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97929 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→50 Å / Num. obs: 78578 / % possible obs: 99.3 % / Redundancy: 13.6 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 36.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5WFU Resolution: 1.651→38.687 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.77
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.651→38.687 Å
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Refine LS restraints |
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LS refinement shell |
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