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Open data
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Basic information
Entry | Database: PDB / ID: 2c23 | ||||||
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Title | 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide | ||||||
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![]() | SIGNALING PROTEIN / 14-3-3 / YWHAB / EXOS / EXOENZYME S / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / ACETYLATION / ALTERNATIVE INITIATION / PHOSPHORYLATION / CELL REGULATOR PROTEIN | ||||||
Function / homology | ![]() negative regulation of protein dephosphorylation / cytoplasmic sequestering of protein / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / negative regulation of G protein-coupled receptor signaling pathway / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / MTOR signalling / ARMS-mediated activation / SHOC2 M1731 mutant abolishes MRAS complex function / Gain-of-function MRAS complexes activate RAF signaling / Rap1 signalling ...negative regulation of protein dephosphorylation / cytoplasmic sequestering of protein / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / negative regulation of G protein-coupled receptor signaling pathway / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / MTOR signalling / ARMS-mediated activation / SHOC2 M1731 mutant abolishes MRAS complex function / Gain-of-function MRAS complexes activate RAF signaling / Rap1 signalling / Signaling by Hippo / vacuolar membrane / Frs2-mediated activation / positive regulation of catalytic activity / protein kinase inhibitor activity / mTORC1-mediated signalling / Regulation of localization of FOXO transcription factors / NAD+-protein poly-ADP-ribosyltransferase activity / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / 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 / nucleotidyltransferase activity / GTPase activator activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / phosphoprotein binding / RAF activation / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / histone deacetylase binding / Negative regulation of MAPK pathway / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / melanosome / toxin activity / cadherin binding / protein domain specific binding / focal adhesion / perinuclear region of cytoplasm / enzyme binding / signal transduction / extracellular exosome / extracellular region / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Elkins, J.M. / Schoch, G.A. / Yang, X. / Sundstrom, M. / Arrowsmith, C. / Edwards, A. / Doyle, D.A. | ||||||
![]() | ![]() Title: Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Authors: Yang, X. / Lee, W.H. / Sobott, F. / Papagrigoriou, E. / Robinson, C.V. / Grossmann, J.G. / Sundstrom, M. / Doyle, D.A. / Elkins, J.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.4 KB | Display | ![]() |
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PDB format | ![]() | 42.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.2 KB | Display | ![]() |
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Full document | ![]() | 437.5 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 13.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bq0SC ![]() 2br9C ![]() 2btpC ![]() 2c63C ![]() 2c74C 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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Unit cell |
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Details | THE PROTEIN IS A DIMER IN SOLUTION, BUT SINCE IN THIS ENTRY IT IS IN COMPLEX WITH A PEPTIDE (CHAIN P), THE ENTRY IS MARKED AS TETRAMERIC |
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Components
#1: Protein | Mass: 28236.627 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1116.287 Da / Num. of mol.: 1 / Fragment: 14-3-3 BINDING REGION, RESIDUES 421-431 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
Sequence details | RESIDUES 240-245 ARE CLONING ARTEFACT FOR CHAIN A. THE UNIPROT CROSS-REFERENCE GIVEN IN THE DBREF ...RESIDUES 240-245 ARE CLONING ARTEFACT FOR CHAIN A. THE UNIPROT CROSS-REFERENCE GIVEN IN THE DBREF RECORDS BELOW CORRESPOND |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 55.9 % |
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Crystal grow | pH: 8 Details: 0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 3, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99188 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→49.33 Å / Num. obs: 9558 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 2.65→2.79 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.43 / Mean I/σ(I) obs: 3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2BQ0 Resolution: 2.65→60.86 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.898 / SU B: 13.677 / SU ML: 0.28 / Cross valid method: THROUGHOUT / ESU R: 0.631 / ESU R Free: 0.35 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 61.64 Å2
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Refinement step | Cycle: LAST / Resolution: 2.65→60.86 Å
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