+Open data
-Basic information
Entry | Database: PDB / ID: 6i2u | ||||||
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Title | Aurora-A kinase domain in complex with Coenzyme A | ||||||
Components | Aurora kinase A | ||||||
Keywords | TRANSFERASE / Aurora A Coenzyme A kinase covalent | ||||||
Function / homology | Function and homology information Interaction between PHLDA1 and AURKA / regulation of centrosome cycle / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / positive regulation of oocyte maturation / spindle pole centrosome / histone H3S10 kinase activity / chromosome passenger complex / pronucleus ...Interaction between PHLDA1 and AURKA / regulation of centrosome cycle / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / positive regulation of oocyte maturation / spindle pole centrosome / histone H3S10 kinase activity / chromosome passenger complex / pronucleus / meiotic spindle / mitotic centrosome separation / germinal vesicle / protein localization to centrosome / anterior/posterior axis specification / centrosome localization / neuron projection extension / spindle organization / positive regulation of mitochondrial fission / mitotic spindle pole / SUMOylation of DNA replication proteins / spindle midzone / regulation of G2/M transition of mitotic cell cycle / centriole / protein serine/threonine/tyrosine kinase activity / positive regulation of mitotic cell cycle / positive regulation of mitotic nuclear division / AURKA Activation by TPX2 / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / mitotic spindle organization / ciliary basal body / regulation of cytokinesis / negative regulation of protein binding / regulation of signal transduction by p53 class mediator / molecular function activator activity / liver regeneration / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / regulation of protein stability / spindle microtubule / mitotic spindle / kinetochore / response to wounding / spindle / G2/M transition of mitotic cell cycle / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / mitotic cell cycle / midbody / basolateral plasma membrane / peptidyl-serine phosphorylation / proteasome-mediated ubiquitin-dependent protein catabolic process / Regulation of TP53 Activity through Phosphorylation / protein autophosphorylation / postsynaptic density / non-specific serine/threonine protein kinase / protein kinase activity / protein heterodimerization activity / cell division / protein phosphorylation / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / glutamatergic synapse / apoptotic process / ubiquitin protein ligase binding / negative regulation of apoptotic process / protein kinase binding / perinuclear region of cytoplasm / nucleoplasm / ATP binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Burgess, S.G. / Bayliss, R. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Redox Biol / Year: 2019 Title: Covalent Aurora A regulation by the metabolic integrator coenzyme A. Authors: Tsuchiya, Y. / Byrne, D.P. / Burgess, S.G. / Bormann, J. / Bakovic, J. / Huang, Y. / Zhyvoloup, A. / Yu, B.Y.K. / Peak-Chew, S. / Tran, T. / Bellany, F. / Tabor, A.B. / Chan, A.E. / ...Authors: Tsuchiya, Y. / Byrne, D.P. / Burgess, S.G. / Bormann, J. / Bakovic, J. / Huang, Y. / Zhyvoloup, A. / Yu, B.Y.K. / Peak-Chew, S. / Tran, T. / Bellany, F. / Tabor, A.B. / Chan, A.E. / Guruprasad, L. / Garifulin, O. / Filonenko, V. / Vonderach, M. / Ferries, S. / Eyers, C.E. / Carroll, J. / Skehel, M. / Bayliss, R. / Eyers, P.A. / Gout, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6i2u.cif.gz | 72.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6i2u.ent.gz | 51.4 KB | Display | PDB format |
PDBx/mmJSON format | 6i2u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i2/6i2u ftp://data.pdbj.org/pub/pdb/validation_reports/i2/6i2u | HTTPS FTP |
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-Related structure data
Related structure data | 4cegS 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: 33108.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Gene: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6 Production host: Escherichia coli (E. coli) References: UniProt: O14965, non-specific serine/threonine protein kinase | ||||
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#2: Chemical | ChemComp-COA / | ||||
#3: Chemical | ChemComp-MG / #4: Chemical | #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: 2.47 Å3/Da / Density % sol: 50.25 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop Details: 0.03 M MgCl2.6H20, 0.03 M CaCl2.2H20, 0.1 M MOPS/HEPES-Na pH 7.5, 20% (v/v) PEG 500 MME, 10% (w/v) PEG 20 000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Feb 14, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→44.58 Å / Num. obs: 12318 / % possible obs: 100 % / Redundancy: 17.6 % / CC1/2: 0.999 / Rmerge(I) obs: 0.086 / Rpim(I) all: 0.021 / Rrim(I) all: 0.088 / Net I/σ(I): 21.9 |
Reflection shell | Resolution: 2.5→2.54 Å / Num. unique obs: 599 / CC1/2: 0.458 / Rpim(I) all: 0.452 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4CEG Resolution: 2.5→44.574 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.29
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→44.574 Å
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Refine LS restraints |
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LS refinement shell |
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