+Open data
-Basic information
Entry | Database: PDB / ID: 3uc4 | ||||||
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Title | The crystal structure of Snf1-related kinase 2.6 | ||||||
Components | Serine/threonine-protein kinase SRK2E | ||||||
Keywords | TRANSFERASE / SnRK2.6 / kinase / ABA signaling | ||||||
Function / homology | Function and homology information cellular response to absence of light / regulation of anion channel activity / regulation of stomatal opening / unsaturated fatty acid biosynthetic process / cellular response to carbon dioxide / triglyceride biosynthetic process / positive regulation of abscisic acid-activated signaling pathway / sucrose metabolic process / regulation of stomatal closure / stomatal movement ...cellular response to absence of light / regulation of anion channel activity / regulation of stomatal opening / unsaturated fatty acid biosynthetic process / cellular response to carbon dioxide / triglyceride biosynthetic process / positive regulation of abscisic acid-activated signaling pathway / sucrose metabolic process / regulation of stomatal closure / stomatal movement / leaf development / regulation of stomatal movement / calcium-dependent protein serine/threonine kinase activity / response to water deprivation / response to abscisic acid / abscisic acid-activated signaling pathway / regulation of reactive oxygen species metabolic process / response to osmotic stress / response to salt stress / kinase activity / protein phosphatase binding / protein autophosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / defense response to bacterium / protein serine kinase activity / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å | ||||||
Authors | Zhou, X.E. / Ng, L.-M. / Soon, F.-F. / Kovach, A. / Suino-Powell, K.M. / Li, J. / Melcher, K. / Xu, H.E. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases. Authors: Ng, L.M. / Soon, F.F. / Zhou, X.E. / West, G.M. / Kovach, A. / Suino-Powell, K.M. / Chalmers, M.J. / Li, J. / Yong, E.L. / Zhu, J.K. / Griffin, P.R. / Melcher, K. / Xu, H.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3uc4.cif.gz | 240 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3uc4.ent.gz | 195.2 KB | Display | PDB format |
PDBx/mmJSON format | 3uc4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uc/3uc4 ftp://data.pdbj.org/pub/pdb/validation_reports/uc/3uc4 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 40994.457 Da / Num. of mol.: 2 / Fragment: Kinase domain / Mutation: D59A, E60A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: SRK2E, OST1, SNRK2.6, At4g33950, F17I5.140 / Plasmid: pET24a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q940H6, non-specific serine/threonine protein kinase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.84 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 7.5 Details: PEG 3350, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 16, 2010 |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 34149 / % possible obs: 91 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.3→2.38 Å / % possible all: 100 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→29.85 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.921 / Occupancy max: 1 / Occupancy min: 1 / SU B: 14.408 / SU ML: 0.158 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.224 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 123.53 Å2 / Biso mean: 48.0162 Å2 / Biso min: 13.35 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→29.85 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.359 Å / Total num. of bins used: 20
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