+Open data
-Basic information
Entry | Database: PDB / ID: 2x81 | ||||||
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Title | STRUCTURE OF AURORA A IN COMPLEX WITH MLN8054 | ||||||
Components | SERINE/THREONINE-PROTEIN KINASE 6Serine/threonine-specific protein kinase | ||||||
Keywords | TRANSFERASE / DRUG-RESISTANCE / CELL CYCLE / CYTOSKELETON | ||||||
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 / spindle pole centrosome / positive regulation of oocyte maturation / 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 / spindle pole centrosome / positive regulation of oocyte maturation / 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 / positive regulation of mitochondrial fission / spindle organization / 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 / AURKA Activation by TPX2 / mitotic spindle organization / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / positive regulation of mitotic nuclear division / ciliary basal body / negative regulation of protein binding / regulation of signal transduction by p53 class mediator / regulation of cytokinesis / 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 / spindle / kinetochore / response to wounding / microtubule cytoskeleton / G2/M transition of mitotic cell cycle / Regulation of PLK1 Activity at G2/M Transition / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / mitotic cell cycle / midbody / proteasome-mediated ubiquitin-dependent protein catabolic process / basolateral plasma membrane / peptidyl-serine phosphorylation / Regulation of TP53 Activity through Phosphorylation / microtubule / postsynaptic density / protein autophosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / protein heterodimerization activity / cell division / negative regulation of gene expression / protein phosphorylation / protein serine kinase activity / centrosome / protein serine/threonine kinase activity / 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 / MOLECULAR REPLACEMENT / Resolution: 2.91 Å | ||||||
Authors | Savory, W. / Mueller, I. / Mason, C.S. / Lamers, M. / Williams, D.H. / Eyers, P.A. | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2010 Title: Drug-Resistant Aurora a Mutants for Cellular Target Validation of the Small Molecule Kinase Inhibitors Mln8054 and Mln8237. Authors: Sloane, D. / Trikic, M. / Chu, M.L. / Lamers, M. / Mason, C.S. / Mueller, I. / Savory, W. / Williams, D.H. / Eyers, P.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x81.cif.gz | 111.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2x81.ent.gz | 86.4 KB | Display | PDB format |
PDBx/mmJSON format | 2x81.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x8/2x81 ftp://data.pdbj.org/pub/pdb/validation_reports/x8/2x81 | HTTPS FTP |
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-Related structure data
Related structure data | 1mq4S 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: 31440.150 Da / Num. of mol.: 1 / Fragment: RESIDUES 126-391 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PSARBAC/TEV / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) References: UniProt: O14965, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-ZZL / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.3 % / Description: NONE |
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Crystal grow | pH: 7.6 Details: 0.2M K2HPO4, 20% PEG3350, 1MM TRIS(HYDROXYPROPYL)PHOSPHINE, pH 7.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 |
Detector | Type: RIGAKU SATURN944 CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.91→24.5 Å / Num. obs: 8043 / % possible obs: 98.3 % / Observed criterion σ(I): 2 / Redundancy: 5.8 % / Biso Wilson estimate: 100 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 2 / % possible all: 96.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MQ4 Resolution: 2.91→24.5 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.876 / SU B: 43.256 / SU ML: 0.377 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.275 / ESU R Free: 0.453 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76.887 Å2
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Refinement step | Cycle: LAST / Resolution: 2.91→24.5 Å
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