+Open data
-Basic information
Entry | Database: PDB / ID: 1jwh | ||||||
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Title | Crystal Structure of Human Protein Kinase CK2 Holoenzyme | ||||||
Components | (Casein kinase ...) x 2 | ||||||
Keywords | TRANSFERASE / casein kinase 2 / CK2 holoenzyme / protein kinase CK2 | ||||||
Function / homology | Function and homology information regulation of DNA binding / adiponectin-activated signaling pathway / positive regulation of activin receptor signaling pathway / endothelial tube morphogenesis / protein kinase regulator activity / negative regulation of viral life cycle / regulation of chromosome separation / positive regulation of aggrephagy / WNT mediated activation of DVL / Condensation of Prometaphase Chromosomes ...regulation of DNA binding / adiponectin-activated signaling pathway / positive regulation of activin receptor signaling pathway / endothelial tube morphogenesis / protein kinase regulator activity / negative regulation of viral life cycle / regulation of chromosome separation / positive regulation of aggrephagy / WNT mediated activation of DVL / Condensation of Prometaphase Chromosomes / protein kinase CK2 complex / symbiont-mediated disruption of host cell PML body / Receptor Mediated Mitophagy / Sin3-type complex / Synthesis of PC / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / negative regulation of blood vessel endothelial cell migration / positive regulation of SMAD protein signal transduction / negative regulation of apoptotic signaling pathway / positive regulation of Wnt signaling pathway / chaperone-mediated protein folding / negative regulation of ubiquitin-dependent protein catabolic process / Signal transduction by L1 / Hsp90 protein binding / peptidyl-threonine phosphorylation / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / PML body / Wnt signaling pathway / Regulation of PTEN stability and activity / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / positive regulation of protein catabolic process / rhythmic process / KEAP1-NFE2L2 pathway / double-strand break repair / protein-macromolecule adaptor activity / kinase activity / positive regulation of cell growth / protein-containing complex assembly / peptidyl-serine phosphorylation / secretory granule lumen / Regulation of TP53 Activity through Phosphorylation / ficolin-1-rich granule lumen / negative regulation of translation / RNA polymerase II-specific DNA-binding transcription factor binding / protein stabilization / regulation of cell cycle / non-specific serine/threonine protein kinase / cell cycle / protein domain specific binding / negative regulation of cell population proliferation / signaling receptor binding / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / DNA damage response / chromatin binding / positive regulation of cell population proliferation / chromatin / Neutrophil degranulation / signal transduction / extracellular exosome / extracellular region / nucleoplasm / ATP binding / identical protein binding / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Niefind, K. / Guerra, B. / Ermakowa, I. / Issinger, O.G. | ||||||
Citation | Journal: EMBO J. / Year: 2001 Title: Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. Authors: Niefind, K. / Guerra, B. / Ermakowa, I. / Issinger, O.G. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: Crystallization and Preliminary Characterization of Crystals of Human Protein Kinase CK2 Authors: Niefind, K. / Guerra, B. / Ermakowa, I. / Issinger, O.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jwh.cif.gz | 244.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jwh.ent.gz | 194.2 KB | Display | PDB format |
PDBx/mmJSON format | 1jwh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jw/1jwh ftp://data.pdbj.org/pub/pdb/validation_reports/jw/1jwh | HTTPS FTP |
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-Related structure data
Related structure data | 1dawS 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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Details | The asymmetric unit contains one complete CK2 tetramer comprising two catalytic and two regulatory subunits. |
-Components
-Casein kinase ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 40240.902 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P68400, EC: 2.7.1.37 #2: Protein | Mass: 24969.412 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P67870 |
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-Non-polymers , 4 types, 219 molecules
#3: Chemical | ChemComp-PO4 / #4: Chemical | ChemComp-ANP / | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.8 % Description: WHILE THE OVERALL DATA COMPLETENESS FOR THE GIVEN RESOLUTION RANGE (59.3 A - 3.1 A) WAS 98.4 % ONLY 78.7 % OF ALL POSSIBLE DATA WERE USED IN REFINEMENT WITH CNS. THE REASON FOR THIS ...Description: WHILE THE OVERALL DATA COMPLETENESS FOR THE GIVEN RESOLUTION RANGE (59.3 A - 3.1 A) WAS 98.4 % ONLY 78.7 % OF ALL POSSIBLE DATA WERE USED IN REFINEMENT WITH CNS. THE REASON FOR THIS DISCREPANCY WAS THAT THE DATA HAD NOT BEEN WILSON SCALED AFTER PROCESSING AND ALL NEGATIVE INTENSITIES HAD BEEN SET TO ZERO WHEN THE INTENSITIES HAD BEEN CONVERTED TO STRUCTURE AMPLITUDES. ALL THESE ZERO DATA WERE IGNORED DURING REFINEMENT WITH CNS. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 285 K / Method: vapor diffusion, sitting drop / pH: 9.3 Details: initial composition of the drop: 3 ul rhCK2 stock solution [5 mg/ml enzyme in 25 mM Tris/HCl, 300 mM NaCl, 1 mM dithiothreitole, pH 8.5], 1.5 ul reservoir solution [20 % (w/v) PEG3350, 200 ...Details: initial composition of the drop: 3 ul rhCK2 stock solution [5 mg/ml enzyme in 25 mM Tris/HCl, 300 mM NaCl, 1 mM dithiothreitole, pH 8.5], 1.5 ul reservoir solution [20 % (w/v) PEG3350, 200 mM dipotassium hydrogenphosphate], 3 ul 1 mM adenylyl imidodiphosphate (AMPPNP), 3 ul 2 mM magnesium chloride, 2 ul 10 % (w/v) polyethylene glycol 400 dodecylether (Thesit), pH 9.3, VAPOR DIFFUSION, SITTING DROP, temperature 285K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 12 ℃ / pH: 8.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8428 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 26, 2000 |
Radiation | Monochromator: silicon 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8428 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→59.3 Å / Num. obs: 29935 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.8 % / Biso Wilson estimate: 92.2 Å2 / Limit h max: 49 / Limit h min: 0 / Limit k max: 48 / Limit k min: 0 / Limit l max: 30 / Limit l min: 0 / Observed criterion F max: 2867098.76 / Observed criterion F min: 1.5 / Rsym value: 0.096 / Net I/σ(I): 16.7 |
Reflection shell | Resolution: 3.1→3.2 Å / Redundancy: 6 % / Mean I/σ(I) obs: 2.6 / Rsym value: 42 / % possible all: 90.4 |
Reflection | *PLUS Num. measured all: 268848 / Rmerge(I) obs: 0.096 |
Reflection shell | *PLUS % possible obs: 90.4 % / Rmerge(I) obs: 0.42 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: POLY-ALANINE BACKBONE OF CK2A FROM ZEA MAYS (PDB ENTRY 1DAW) Resolution: 3.1→59.3 Å / Rfactor Rfree error: 0.011 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
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Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 27.2984 Å2 / ksol: 0.269435 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 243.39 Å2 / Biso mean: 90.96 Å2 / Biso min: 3.08 Å2
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Refine Biso |
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.1→59.3 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 60 Å / σ(F): 0 / % reflection Rfree: 4 % / Rfactor obs: 0.267 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 91 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.458 / % reflection Rfree: 2.2 % / Rfactor Rwork: 0.458 |