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Yorodumi- PDB-3p1o: Crystal structure of human 14-3-3 sigma in complex with TASK-3 pe... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3p1o | ||||||
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Title | Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilisator Fusicoccin A | ||||||
Components |
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Keywords | PEPTIDE BINDING PROTEIN / Helical protein / Phosphoprotein / Adapter protein / Nucleus | ||||||
Function / homology | Function and homology information TWIK-releated acid-sensitive K+ channel (TASK) / Phase 4 - resting membrane potential / stabilization of membrane potential / potassium ion leak channel activity / outward rectifier potassium channel activity / regulation of epidermal cell division / protein kinase C inhibitor activity / potassium ion import across plasma membrane / positive regulation of epidermal cell differentiation / keratinocyte development ...TWIK-releated acid-sensitive K+ channel (TASK) / Phase 4 - resting membrane potential / stabilization of membrane potential / potassium ion leak channel activity / outward rectifier potassium channel activity / regulation of epidermal cell division / protein kinase C inhibitor activity / potassium ion import across plasma membrane / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / potassium channel activity / 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 / protein kinase A signaling / negative regulation of stem cell proliferation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / potassium ion transmembrane transport / protein export from nucleus / negative regulation of innate immune response / protein sequestering activity / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / release of cytochrome c from mitochondria / positive regulation of protein export from nucleus / 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 / potassium ion transport / intrinsic apoptotic signaling pathway in response to DNA damage / synaptic vesicle / positive regulation of cell growth / regulation of cell cycle / cadherin binding / protein kinase binding / negative regulation of transcription by RNA polymerase II / signal transduction / extracellular space / extracellular exosome / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Anders, C. / Higuchi, Y. / Schumacher, B. / Thiel, P. / Kato, N. / Ottmann, C. | ||||||
Citation | Journal: Chem. Biol. / Year: 2013 Title: A semisynthetic fusicoccane stabilizes a protein-protein interaction and enhances the expression of K+ channels at the cell surface Authors: Anders, C. / Higuchi, Y. / Koschinsky, K. / Bartel, M. / Schumacher, B. / Thiel, P. / Nitta, H. / Preisig-Muller, R. / Schlichthorl, G. / Renigunta, V. / Ohkanda, J. / Daut, J. / Kato, N. / Ottmann, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3p1o.cif.gz | 74.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3p1o.ent.gz | 54 KB | Display | PDB format |
PDBx/mmJSON format | 3p1o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p1/3p1o ftp://data.pdbj.org/pub/pdb/validation_reports/p1/3p1o | HTTPS FTP |
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-Related structure data
Related structure data | 3p1nC 3p1pC 3p1qC 3p1rC 3p1sC 3smkC 3smlC 3smmC 3smnC 3smoC 3sp5C 3sprC 3ux0C 4fr3C 3lw1S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein / Protein/peptide , 2 types, 2 molecules AP
#1: Protein | Mass: 26501.865 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SFN / Plasmid: pPROEX HTB / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta DE3 / References: UniProt: P31947 |
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#2: Protein/peptide | Mass: 856.950 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: Q9NPC2 |
-Non-polymers , 5 types, 212 molecules
#3: Chemical | ChemComp-FSC / | ||
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#4: Chemical | ChemComp-CL / | ||
#5: Chemical | ChemComp-CA / | ||
#6: Chemical | ChemComp-MG / #7: 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: 2.62 Å3/Da / Density % sol: 52.97 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.5418 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Nov 25, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→45.4 Å / Num. all: 23013 / Num. obs: 22884 / % possible obs: 99.4 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 5.96 % / Biso Wilson estimate: 25.436 Å2 / Rmerge(I) obs: 0.103 / Net I/σ(I): 17.69 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 4.55 % / Rmerge(I) obs: 0.451 / Mean I/σ(I) obs: 4.04 / Num. unique all: 3220 / % possible all: 99.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB Entry 3LW1 Resolution: 1.9→42.05 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.91 / SU B: 3.031 / SU ML: 0.091 / Cross valid method: THROUGHOUT / ESU R: 0.146 / ESU R Free: 0.148 / 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: 20.458 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→42.05 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.949 Å / Total num. of bins used: 20
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