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- PDB-6cpf: Structure of dephosphorylated Aurora A (122-403) bound to AMPPCP ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6cpf | |||||||||||||||
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Title | Structure of dephosphorylated Aurora A (122-403) bound to AMPPCP in an active conformation | |||||||||||||||
![]() | Aurora kinase A | |||||||||||||||
![]() | TRANSFERASE / protein kinase / DFG-loop / cell cycle | |||||||||||||||
Function / homology | ![]() 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 / mitotic centrosome separation / meiotic spindle / 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 / AURKA Activation by TPX2 / positive regulation of mitotic nuclear division / positive regulation of mitotic cell cycle / mitotic spindle organization / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / ciliary basal body / regulation of cytokinesis / regulation of signal transduction by p53 class mediator / negative regulation of protein binding / 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 / 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 / peptidyl-serine phosphorylation / basolateral plasma membrane / proteasome-mediated ubiquitin-dependent protein catabolic process / Regulation of TP53 Activity through Phosphorylation / microtubule / 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 / ubiquitin protein ligase binding / negative regulation of apoptotic process / apoptotic process / protein kinase binding / perinuclear region of cytoplasm / nucleoplasm / ATP binding / nucleus / cytosol Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||
![]() | Otten, R. / Zorba, A. / Padua, R.A.P. / Kern, D. | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Dynamics of human protein kinase Aurora A linked to drug selectivity. Authors: Pitsawong, W. / Buosi, V. / Otten, R. / Agafonov, R.V. / Zorba, A. / Kern, N. / Kutter, S. / Kern, G. / Padua, R.A. / Meniche, X. / Kern, D. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136 KB | Display | ![]() |
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PDB format | ![]() | 86.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6cpeC ![]() 6cpgC ![]() 1mq4S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 32990.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6 Plasmid: pET28a / Production host: ![]() ![]() References: UniProt: O14965, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-ACP / |
#3: Chemical | ChemComp-MG / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.74 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Crystals were obtained by mixing 570 uM Aurora A (18 mg/mL) in buffer (20 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20 mM MgCl2, 1 mM TCEP) in a 2:1 ratio with mother liquor (0.2 M Tris-HCl, pH 7.5, ...Details: Crystals were obtained by mixing 570 uM Aurora A (18 mg/mL) in buffer (20 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20 mM MgCl2, 1 mM TCEP) in a 2:1 ratio with mother liquor (0.2 M Tris-HCl, pH 7.5, 0.2 M ammonium sulfate, 30% (w/v) PEG-3350). |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 17, 2012 |
Radiation | Monochromator: DOUBLE CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.999941 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→86.44 Å / Num. all: 154145 / Num. obs: 15873 / % possible obs: 100 % / Redundancy: 9.7 % / Biso Wilson estimate: 55.9 Å2 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 2.3→2.39 Å / Num. unique all: 1613 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1MQ4 Resolution: 2.3→54.79 Å / SU ML: 0.3526 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.2215
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 69.63 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→54.79 Å
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Refine LS restraints |
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LS refinement shell |
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