+Open data
-Basic information
Entry | Database: PDB / ID: 6a1c | ||||||
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Title | Crystal structure of the CK2a1-go289 complex | ||||||
Components | Casein kinase II subunit alphaCasein kinase 2 | ||||||
Keywords | TRANSFERASE / CK2a1 / Inhibitor / Complex | ||||||
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: 1.68 Å | ||||||
Authors | Kinoshita, T. / Tsuyuguchi, M. | ||||||
Citation | Journal: Sci Adv / Year: 2019 Title: Cell-based screen identifies a new potent and highly selective CK2 inhibitor for modulation of circadian rhythms and cancer cell growth. Authors: Oshima, T. / Niwa, Y. / Kuwata, K. / Srivastava, A. / Hyoda, T. / Tsuchiya, Y. / Kumagai, M. / Tsuyuguchi, M. / Tamaru, T. / Sugiyama, A. / Ono, N. / Zolboot, N. / Aikawa, Y. / Oishi, S. / ...Authors: Oshima, T. / Niwa, Y. / Kuwata, K. / Srivastava, A. / Hyoda, T. / Tsuchiya, Y. / Kumagai, M. / Tsuyuguchi, M. / Tamaru, T. / Sugiyama, A. / Ono, N. / Zolboot, N. / Aikawa, Y. / Oishi, S. / Nonami, A. / Arai, F. / Hagihara, S. / Yamaguchi, J. / Tama, F. / Kunisaki, Y. / Yagita, K. / Ikeda, M. / Kinoshita, T. / Kay, S.A. / Itami, K. / Hirota, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6a1c.cif.gz | 171.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6a1c.ent.gz | 133.1 KB | Display | PDB format |
PDBx/mmJSON format | 6a1c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/6a1c ftp://data.pdbj.org/pub/pdb/validation_reports/a1/6a1c | HTTPS FTP |
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-Related structure data
Related structure data | 3warS 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: 40478.191 Da / Num. of mol.: 1 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 | ||
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#2: Chemical | ChemComp-9NX / | ||
#3: Chemical | ChemComp-NA / | ||
#4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.41 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: ethyleneglycol |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Apr 18, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.68→55.95 Å / Num. obs: 37267 / % possible obs: 99.6 % / Redundancy: 7.3 % / Rmerge(I) obs: 0.056 / Net I/σ(I): 30.6 |
Reflection shell | Resolution: 1.68→1.71 Å / Redundancy: 7.1 % / Rmerge(I) obs: 0.462 / Mean I/σ(I) obs: 5.7 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3war Resolution: 1.68→55.94 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.951 / SU B: 4.409 / SU ML: 0.066 / Cross valid method: THROUGHOUT / ESU R: 0.156 / ESU R Free: 0.1 / 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: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.406 Å2
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Refinement step | Cycle: 1 / Resolution: 1.68→55.94 Å
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Refine LS restraints |
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