+Open data
-Basic information
Entry | Database: PDB / ID: 5csp | ||||||
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Title | Crystal Structure of CK2alpha with Compound 5 bound | ||||||
Components | Casein kinase II subunit alpha | ||||||
Keywords | TRANSFERASE / CK2alpha / CK2a / fragment based drug discovery / high concentration screening / selective ATP competitive inhibitors / surface entrophy reduction | ||||||
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 / Maturation of hRSV A proteins / negative regulation of apoptotic signaling pathway / positive regulation of Wnt signaling pathway / negative regulation of double-strand break repair via homologous recombination / chaperone-mediated protein folding / negative regulation of ubiquitin-dependent protein catabolic process / Signal transduction by L1 / peptidyl-threonine phosphorylation / Hsp90 protein binding / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / PML body / Wnt signaling pathway / Regulation of PTEN stability and activity / positive regulation of protein catabolic process / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / KEAP1-NFE2L2 pathway / double-strand break repair / rhythmic process / kinase activity / positive regulation of cell growth / peptidyl-serine phosphorylation / Regulation of TP53 Activity through Phosphorylation / protein stabilization / negative regulation of translation / non-specific serine/threonine protein kinase / regulation of cell cycle / 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 / molecular replacement / Resolution: 1.5 Å | ||||||
Authors | Brear, P. / De Fusco, C. / Georgiou, K.H. / Spring, D. / Hyvonen, M. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Chem Sci / Year: 2016 Title: Specific inhibition of CK2 alpha from an anchor outside the active site. Authors: Brear, P. / De Fusco, C. / Hadje Georgiou, K. / Francis-Newton, N.J. / Stubbs, C.J. / Sore, H.F. / Venkitaraman, A.R. / Abell, C. / Spring, D.R. / Hyvonen, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5csp.cif.gz | 156.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5csp.ent.gz | 122.4 KB | Display | PDB format |
PDBx/mmJSON format | 5csp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5csp_validation.pdf.gz | 455.5 KB | Display | wwPDB validaton report |
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Full document | 5csp_full_validation.pdf.gz | 457.9 KB | Display | |
Data in XML | 5csp_validation.xml.gz | 16.8 KB | Display | |
Data in CIF | 5csp_validation.cif.gz | 25.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/5csp ftp://data.pdbj.org/pub/pdb/validation_reports/cs/5csp | HTTPS FTP |
-Related structure data
Related structure data | 5clpC 5cs6C 5cshC 5csvC 5cu3C 5cu4C 5cu6C 5cvfC 5cvgC 5cvhC 3warS S: Starting model for refinement C: citing same article (ref.) |
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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: 39031.391 Da / Num. of mol.: 1 / Fragment: UNP residues 2-329 / Mutation: R21S, K74A, K75A, K76A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CSNK2A1, CK2A1 / Plasmid: pHAT2 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P68400, non-specific serine/threonine protein kinase | ||
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#2: Chemical | ChemComp-54G / | ||
#3: Chemical | #4: 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: 2.02 Å3/Da / Density % sol: 39.13 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 112.5mM Mes pH 6.5, 35% glycerol ethoxylate, 180 mM ammonium acetate |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92 Å | |||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 13, 2014 | |||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 | |||||||||||||||||||||||||||
Reflection | Resolution: 1.5→54.47 Å / Num. obs: 39484 / % possible obs: 78.4 % / Redundancy: 3.2 % / Biso Wilson estimate: 17.39 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.025 / Rpim(I) all: 0.016 / Net I/σ(I): 29.3 / Num. measured all: 125113 / Scaling rejects: 1 | |||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3WAR Resolution: 1.5→54.47 Å / Cor.coef. Fo:Fc: 0.9609 / Cor.coef. Fo:Fc free: 0.9545 / SU R Cruickshank DPI: 0.09 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.093 / SU Rfree Blow DPI: 0.087 / SU Rfree Cruickshank DPI: 0.085
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Displacement parameters | Biso max: 123.92 Å2 / Biso mean: 22.16 Å2 / Biso min: 3.9 Å2
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Refine analyze | Luzzati coordinate error obs: 0.163 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.5→54.47 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.53 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 79.9633 Å / Origin y: 9.2996 Å / Origin z: 133.6369 Å
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Refinement TLS group | Selection details: { A|* } |