+Open data
-Basic information
Entry | Database: PDB / ID: 4pwn | ||||||
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Title | Crystal structure of Active WNK1 kinase | ||||||
Components | Serine/threonine-protein kinase WNK1 | ||||||
Keywords | TRANSFERASE / kinase / WNK1 / Ser/Thr protein kinase / Serine/Threonine kinase / ATP-binding / phosphorylation | ||||||
Function / homology | Function and homology information negative regulation of cell-cell adhesion mediated by integrin / lymphocyte migration into lymph node / chemokine (C-C motif) ligand 21 signaling pathway / positive regulation of termination of RNA polymerase II transcription / monoatomic cation homeostasis / negative regulation of pancreatic juice secretion / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / positive regulation of mitotic cytokinesis / negative regulation of sodium ion transport / regulation of mRNA export from nucleus ...negative regulation of cell-cell adhesion mediated by integrin / lymphocyte migration into lymph node / chemokine (C-C motif) ligand 21 signaling pathway / positive regulation of termination of RNA polymerase II transcription / monoatomic cation homeostasis / negative regulation of pancreatic juice secretion / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / positive regulation of mitotic cytokinesis / negative regulation of sodium ion transport / regulation of mRNA export from nucleus / regulation of sodium ion transmembrane transport / intracellular chloride ion homeostasis / negative regulation of heterotypic cell-cell adhesion / non-membrane-bounded organelle assembly / positive regulation of T cell chemotaxis / positive regulation of systemic arterial blood pressure / potassium ion homeostasis / cellular hyperosmotic response / cellular response to chemokine / negative regulation of leukocyte cell-cell adhesion / regulation of monoatomic cation transmembrane transport / cell volume homeostasis / negative regulation of protein localization to plasma membrane / negative regulation of GTPase activity / intracellular non-membrane-bounded organelle / protein kinase activator activity / sodium ion transmembrane transport / neuron development / phosphatase binding / monoatomic ion transport / regulation of sodium ion transport / negative regulation of protein ubiquitination / molecular condensate scaffold activity / negative regulation of autophagy / peptidyl-threonine phosphorylation / Stimuli-sensing channels / mitotic spindle / positive regulation of canonical Wnt signaling pathway / positive regulation of angiogenesis / heart development / T cell receptor signaling pathway / peptidyl-serine phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein kinase binding / signal transduction / protein-containing complex / ATP binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.84 Å | ||||||
Authors | Piala, A. / Moon, T. / Akella, T. / He, H. / Cobbm, M.H. / Goldsmith, E. | ||||||
Citation | Journal: Sci.Signal. / Year: 2014 Title: Chloride Sensing by WNK1 Involves Inhibition of Autophosphorylation. Authors: Piala, A.T. / Moon, T.M. / Akella, R. / He, H. / Cobb, M.H. / Goldsmith, E.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4pwn.cif.gz | 119.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4pwn.ent.gz | 91.8 KB | Display | PDB format |
PDBx/mmJSON format | 4pwn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pw/4pwn ftp://data.pdbj.org/pub/pdb/validation_reports/pw/4pwn | HTTPS FTP |
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-Related structure data
Related structure data | 4q2aC 3fpq 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
#1: Protein | Mass: 31538.545 Da / Num. of mol.: 1 / Fragment: Serine/Threonine Protein kinase WNK1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: WNK1, HSN2, KDP, KIAA0344, PRKWNK1 / Production host: Escherichia coli (E. coli) References: UniProt: Q9H4A3, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 35.79 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 0.35M potassium phosphate, 19% PEG 3350, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 18, 2010 / Details: mirrors |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→35.18 Å / Num. all: 75996 / Num. obs: 19568 / % possible obs: 99.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 30.9 Å2 / Rmerge(I) obs: 0.05 / Rsym value: 0.05 / Net I/σ(I): 30.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 3FPQ 3fpq Resolution: 1.84→35.18 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.925 / SU B: 10.651 / SU ML: 0.159 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / ESU R: 0.195 / ESU R Free: 0.173 / 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: 48.493 Å2
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Refinement step | Cycle: LAST / Resolution: 1.84→35.18 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.837→1.885 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 13.4357 Å / Origin y: -0.1921 Å / Origin z: 11.6164 Å
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