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- PDB-5okf: CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5okf | ||||||||||||
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Title | CH1 chimera of human 14-3-3 sigma with the HSPB6 phosphopeptide in a conformation with self-bound phosphopeptides | ||||||||||||
![]() | 14-3-3 protein sigma,Heat shock protein beta-6 | ||||||||||||
![]() | SIGNALING PROTEIN / 14-3-3 proteins / Protein chimera / phosphopeptide-binding | ||||||||||||
Function / homology | ![]() structural constituent of eye lens / regulation of epidermal cell division / protein kinase C inhibitor activity / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / Regulation of localization of FOXO transcription factors / keratinocyte proliferation / phosphoserine residue binding / Activation of BAD and translocation to mitochondria ...structural constituent of eye lens / regulation of epidermal cell division / protein kinase C inhibitor activity / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / Regulation of localization of FOXO transcription factors / keratinocyte proliferation / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / negative regulation of keratinocyte proliferation / establishment of skin barrier / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / chaperone-mediated protein folding / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / negative regulation of stem cell proliferation / protein folding chaperone / RHO GTPases activate PKNs / protein kinase A signaling / protein sequestering activity / negative regulation of innate immune response / protein export from nucleus / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / positive regulation of protein export from nucleus / release of cytochrome c from mitochondria / stem cell proliferation / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / negative regulation of protein kinase activity / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of angiogenesis / intrinsic apoptotic signaling pathway in response to DNA damage / unfolded protein binding / protein-folding chaperone binding / response to heat / protein refolding / positive regulation of cell growth / regulation of cell cycle / nuclear speck / cadherin binding / negative regulation of apoptotic process / protein kinase binding / negative regulation of transcription by RNA polymerase II / signal transduction / protein homodimerization activity / mitochondrion / extracellular space / extracellular exosome / extracellular region / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Sluchanko, N.N. / Tugaeva, K.V. / Greive, S.J. / Antson, A.A. | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners. Authors: Sluchanko, N.N. / Tugaeva, K.V. / Greive, S.J. / Antson, A.A. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 709.5 KB | Display | ![]() |
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PDB format | ![]() | 596.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.3 KB | Display | ![]() |
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Full document | ![]() | 478.3 KB | Display | |
Data in XML | ![]() | 32.6 KB | Display | |
Data in CIF | ![]() | 44.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ok9C ![]() 5om0C ![]() 5omaC ![]() 5lu1S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27508.893 Da / Num. of mol.: 4 Fragment: Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12- ...Fragment: Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19,Phosphopeptide, UNP Residues 12-19 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-CD / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.95 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.1 M HEPES buffer (pH 7.5), 1 M Naacetate, and 50 mM cadmium sulfate |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 2, 2016 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 3.14→48 Å / Num. obs: 21607 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 6.469 % / Biso Wilson estimate: 46.79 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.464 / Rrim(I) all: 0.505 / Χ2: 1.144 / Net I/σ(I): 4.2 / Num. measured all: 139771 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5LU1 Resolution: 3.2→48 Å / Cor.coef. Fo:Fc: 0.891 / Cor.coef. Fo:Fc free: 0.896 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.523
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Displacement parameters | Biso max: 189.96 Å2 / Biso mean: 67.73 Å2 / Biso min: 3 Å2
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Refine analyze | Luzzati coordinate error obs: 0.54 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.2→48 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.2→3.37 Å / Rfactor Rfree error: 0 / Total num. of bins used: 10
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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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