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Open data
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Basic information
Entry | Database: PDB / ID: 4czt | ||||||
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Title | Crystal structure of the kinase domain of CIPK23 | ||||||
![]() | CBL-INTERACTING SERINE/THREONINE-PROTEIN KINASE 23 | ||||||
![]() | TRANSFERASE / POTASSIUM TRANSPORT / SNRK3 | ||||||
Function / homology | ![]() stomatal movement / regulation of stomatal movement / response to water deprivation / plastid / potassium channel activity / potassium ion import across plasma membrane / response to nutrient / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity ...stomatal movement / regulation of stomatal movement / response to water deprivation / plastid / potassium channel activity / potassium ion import across plasma membrane / response to nutrient / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / signal transduction / ATP binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chaves-Sanjuan, A. / Sanchez-Barrena, M.J. / Albert, A. | ||||||
![]() | ![]() Title: Structural Basis of the Regulatory Mechanism of the Plant Cipk Family of Protein Kinases Controlling Ion Homeostasis and Abiotic Stress Authors: Chaves-Sanjuan, A. / Sanchez-Barrena, M.J. / Gonzalez-Rubio, J.M. / Moreno, M. / Ragel, P. / Jimenez, M. / Pardo, J.M. / Martinez-Ripoll, M. / Quintero, F.J. / Albert, 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 | ![]() | 273.8 KB | Display | ![]() |
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PDB format | ![]() | 217.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 51.9 KB | Display | |
Data in CIF | ![]() | 72.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4czuC ![]() 4d28C ![]() 3h4jS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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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: 51816.375 Da / Num. of mol.: 4 / Fragment: KINASE DOMAIN, RESIDUES 24-482 Source method: isolated from a genetically manipulated source Details: RESIDUES 19 TO 23 DO NOT CORRESPOND TO SNRK3. 23 AT1G30270 RESIDUES. THESE RESIDUES COMES FROM THE PGEX4T2 EXPRESSION VECTOR. Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q93VD3, non-specific serine/threonine protein kinase #2: Chemical | ChemComp-CPS / #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | Sequence details | RESIDUES 19 TO 23 DO NOT CORRESPOND TO SNRK3.23 AT1G30270 RESIDUES. THESE RESIDUES COMES FROM THE ...RESIDUES 19 TO 23 DO NOT CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % / Description: NONE |
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Crystal grow | Method: microbatch Details: 16 MM CHAPS 0.1 M HEPES PH 7.5, 3.5 M AMMONIUM SULFATE AS PRECIPITANT MIXED WITH THE PROTEIN AT 14 MG/ML USING MICROBATCH METHOD. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 26, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→59.3 Å / Num. obs: 61816 / % possible obs: 99 % / Observed criterion σ(I): 3 / Redundancy: 13.2 % / Biso Wilson estimate: 32.88 Å2 / Rmerge(I) obs: 0.18 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 12.4 % / Rmerge(I) obs: 1.15 / Mean I/σ(I) obs: 3 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3H4J Resolution: 2.3→59.262 Å / SU ML: 0.27 / σ(F): 1.34 / Phase error: 23.44 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→59.262 Å
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Refine LS restraints |
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LS refinement shell |
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