+Open data
-Basic information
Entry | Database: PDB / ID: 6y40 | ||||||
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Title | 14-3-3 Sigma in complex with phosphorylated PLN peptide | ||||||
Components |
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Keywords | PROTEIN BINDING / 14-3-3 / PLN / complex / protein / protein-protein interactions | ||||||
Function / homology | Function and homology information regulation of ATPase-coupled calcium transmembrane transporter activity / negative regulation of calcium ion binding / negative regulation of calcium ion import into sarcoplasmic reticulum / regulation of relaxation of cardiac muscle / negative regulation of ATPase-coupled calcium transmembrane transporter activity / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex / regulation of cardiac muscle cell membrane potential / negative regulation of calcium ion transmembrane transporter activity ...regulation of ATPase-coupled calcium transmembrane transporter activity / negative regulation of calcium ion binding / negative regulation of calcium ion import into sarcoplasmic reticulum / regulation of relaxation of cardiac muscle / negative regulation of ATPase-coupled calcium transmembrane transporter activity / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex / regulation of cardiac muscle cell membrane potential / negative regulation of calcium ion transmembrane transporter activity / acrosome assembly / negative regulation of calcium ion import / negative regulation of catalytic activity / ATPase inhibitor activity / regulation of the force of heart contraction / negative regulation of ATP-dependent activity / cardiac muscle tissue development / regulation of cardiac muscle cell contraction / blood circulation / enzyme inhibitor activity / relaxation of cardiac muscle / regulation of heart contraction / negative regulation of heart rate / muscle cell cellular homeostasis / regulation of epidermal cell division / protein kinase C inhibitor activity / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / regulation of calcium ion transport / Ion transport by P-type ATPases / negative regulation of calcium ion transport / 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 / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / 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 / negative regulation of stem cell proliferation / Ion homeostasis / RHO GTPases activate PKNs / Notch signaling pathway / protein kinase A signaling / sarcoplasmic reticulum membrane / protein sequestering activity / regulation of cytosolic calcium ion concentration / 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 / sarcoplasmic reticulum / Translocation of SLC2A4 (GLUT4) to the plasma membrane / mitochondrial membrane / TP53 Regulates Metabolic Genes / negative regulation of protein kinase activity / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / intracellular calcium ion homeostasis / intrinsic apoptotic signaling pathway in response to DNA damage / ATPase binding / positive regulation of cell growth / regulation of cell cycle / cadherin binding / endoplasmic reticulum membrane / protein kinase binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / signal transduction / protein homodimerization activity / mitochondrion / extracellular space / extracellular exosome / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Ballone, A. / Lau, R.A. / Zweipfenning, F.P.A. / Ottmann, C. | ||||||
Funding support | Netherlands, 1items
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Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2020 Title: A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes. Authors: Ballone, A. / Lau, R.A. / Zweipfenning, F.P.A. / Ottmann, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6y40.cif.gz | 94 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6y40.ent.gz | 55.9 KB | Display | PDB format |
PDBx/mmJSON format | 6y40.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6y40_validation.pdf.gz | 429.5 KB | Display | wwPDB validaton report |
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Full document | 6y40_full_validation.pdf.gz | 429.8 KB | Display | |
Data in XML | 6y40_validation.xml.gz | 16.6 KB | Display | |
Data in CIF | 6y40_validation.cif.gz | 27.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y4/6y40 ftp://data.pdbj.org/pub/pdb/validation_reports/y4/6y40 | HTTPS FTP |
-Related structure data
Related structure data | 6y3mC 6y3oC 6y3rC 6y3sC 6y3vC 6y44C 6y8aC 6y8bC 6y8dC 6y8eC 3lw1S S: Starting model for refinement C: citing same article (ref.) |
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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 on special symmetry positions |
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-Components
#1: Protein/peptide | Mass: 1948.166 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P26678*PLUS | ||||||
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#2: Protein | Mass: 28226.518 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SFN, HME1 / Production host: Escherichia coli (E. coli) / References: UniProt: P31947 | ||||||
#3: Chemical | #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.7 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: PEG400, 1.25% glycerol, 0.2M CaCl, 0.1M HEPES pH 7.5, 2mM BME |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: RIGAKU / Wavelength: 1.541 Å |
Detector | Type: DECTRIS PILATUS 200K / Detector: PIXEL / Date: Oct 16, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.541 Å / Relative weight: 1 |
Reflection | Resolution: 1.59→41.81 Å / Num. obs: 31591 / % possible obs: 80.2 % / Biso Wilson estimate: 9.62 Å2 / CC1/2: 0.996 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 1.59→1.63 Å / Num. unique obs: 31591 / CC1/2: 0.937 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3LW1 Resolution: 1.75→41.81 Å / SU ML: 0.1565 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 19.4398
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.59 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→41.81 Å
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Refine LS restraints |
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LS refinement shell |
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