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Yorodumi- PDB-7b8i: Tetragonal structure of human protein kinase CK2 catalytic subuni... -
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-Basic information
Entry | Database: PDB / ID: 7b8i | |||||||||
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Title | Tetragonal structure of human protein kinase CK2 catalytic subunit in complex with a heparin oligo saccharide | |||||||||
Components | Casein kinase II subunit alphaCasein kinase 2 | |||||||||
Keywords | TRANSFERASE / protein kinase CK2 / casein kinase 2 / catalytic subunit CK2alpha / heparin | |||||||||
Function / homology | Function and homology information 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 ...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 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 / kinase activity / positive regulation of cell growth / peptidyl-serine phosphorylation / Regulation of TP53 Activity through Phosphorylation / negative regulation of translation / protein stabilization / regulation of cell cycle / non-specific serine/threonine protein kinase / cell cycle / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / DNA damage response / positive regulation of cell population proliferation / signal transduction / nucleoplasm / ATP binding / identical protein binding / nucleus / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å | |||||||||
Authors | Niefind, K. / Schnitzler, A. | |||||||||
Funding support | Germany, 2items
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Citation | Journal: Eur.J.Med.Chem. / Year: 2021 Title: Structural basis for the design of bisubstrate inhibitors of protein kinase CK2 provided by complex structures with the substrate-competitive inhibitor heparin. Authors: Schnitzler, A. / Niefind, K. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7b8i.cif.gz | 300.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7b8i.ent.gz | 247.2 KB | Display | PDB format |
PDBx/mmJSON format | 7b8i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b8/7b8i ftp://data.pdbj.org/pub/pdb/validation_reports/b8/7b8i | HTTPS FTP |
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-Related structure data
Related structure data | 7b8hC 2pvrS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 40066.742 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CSNK2A1, CK2A1 / Production host: Escherichia coli (E. coli) References: UniProt: P68400, non-specific serine/threonine protein kinase #2: Polysaccharide | 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid- ...2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid | Type: oligosaccharide / Mass: 2327.897 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-GOL / | #4: Chemical | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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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: 3.22 Å3/Da / Density % sol: 61.78 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop Details: Prior to crystallization, the enzyme was incubated with heparin decasaccharide; the composition of this preincubation solution was 5 mg/ml CK2alpha1-335, 1.4 mM Heparin decasaccharide, 340 ...Details: Prior to crystallization, the enzyme was incubated with heparin decasaccharide; the composition of this preincubation solution was 5 mg/ml CK2alpha1-335, 1.4 mM Heparin decasaccharide, 340 mM NaCl, 25 mM Tris/HCl, pH 8.5. 4 microliter of this enzyme/heparin mixture was mixed with 1 microliter reservoir solution. The composition of the reservoir solution was 32 % (w/v) PEG4000, 0.2 M Lithium sulfate, 0.1 M Tris/HCl, pH 7.5. As a preparation of X-ray diffraction data collection, the crystals were transferred to a cryo solution composed of 32 % (w/v) PEG4000, 10 % (v/v) glycerol, 0.2 M lithium sulfate, 0.5 mM Heparin decasaccharide, 0.1 M Tris/HCl, pH 7.5. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.97795 Å |
Detector | Type: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Jun 5, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97795 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→45.4 Å / Num. obs: 33919 / % possible obs: 98.43 % / Redundancy: 6.7 % / Biso Wilson estimate: 48.47 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.08534 / Rpim(I) all: 0.03554 / Rrim(I) all: 0.09263 / Rsym value: 0.08534 / Net I/σ(I): 16.16 |
Reflection shell | Resolution: 2.55→2.642 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.7234 / Mean I/σ(I) obs: 2.57 / Num. unique obs: 3259 / CC1/2: 0.802 / Rpim(I) all: 0.3073 / Rrim(I) all: 0.7877 / Rsym value: 0.7234 / % possible all: 96.19 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2PVR Resolution: 2.55→45.397 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.94
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.55→45.397 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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