+Open data
-Basic information
Entry | Database: PDB / ID: 2x6e | ||||||
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Title | Aurora-A bound to an inhibitor | ||||||
Components | SERINE/THREONINE-PROTEIN KINASE 6Serine/threonine-specific protein kinase | ||||||
Keywords | TRANSFERASE / MITOSIS / CELL CYCLE | ||||||
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 / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.35 Å | ||||||
Authors | Kosmopoulou, M. / Bayliss, R. | ||||||
Citation | Journal: J. Med. Chem. / Year: 2010 Title: Imidazo[4,5-b]pyridine derivatives as inhibitors of Aurora kinases: lead optimization studies toward the identification of an orally bioavailable preclinical development candidate. Authors: Bavetsias, V. / Large, J.M. / Sun, C. / Bouloc, N. / Kosmopoulou, M. / Matteucci, M. / Wilsher, N.E. / Martins, V. / Reynisson, J. / Atrash, B. / Faisal, A. / Urban, F. / Valenti, M. / de ...Authors: Bavetsias, V. / Large, J.M. / Sun, C. / Bouloc, N. / Kosmopoulou, M. / Matteucci, M. / Wilsher, N.E. / Martins, V. / Reynisson, J. / Atrash, B. / Faisal, A. / Urban, F. / Valenti, M. / de Haven Brandon, A. / Box, G. / Raynaud, F.I. / Workman, P. / Eccles, S.A. / Bayliss, R. / Blagg, J. / Linardopoulos, S. / McDonald, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x6e.cif.gz | 66.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2x6e.ent.gz | 47.3 KB | Display | PDB format |
PDBx/mmJSON format | 2x6e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x6/2x6e ftp://data.pdbj.org/pub/pdb/validation_reports/x6/2x6e | HTTPS FTP |
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-Related structure data
Related structure data | 2x6dC 1mq4S C: citing same article (ref.) 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: 32948.781 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 122-403 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: O14965, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-YM4 / |
Sequence details | N-TERMINAL 'GAM' APPENDED FROM VECTOR SEQUENCE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 51 % / Description: NONE |
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Crystal grow | Details: 0.1 M NACL, 0.1 M HEPES, PH 7.5 1.6 M AMMONIUM SULFATE. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Type: ESRF / Wavelength: 0.9721 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9721 Å / Relative weight: 1 |
Reflection | Resolution: 3.35→72.1 Å / Num. obs: 5271 / % possible obs: 100 % / Observed criterion σ(I): 6 / Redundancy: 12.7 % / Biso Wilson estimate: 113.27 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 18.4 |
Reflection shell | Resolution: 3.35→3.53 Å / Redundancy: 8 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 7.6 / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MQ4 Resolution: 3.35→19.996 Å / SU ML: 1.69 / σ(F): 0.06 / Phase error: 32.79 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 96.699 Å2 / ksol: 0.362 e/Å3 | ||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.35→19.996 Å
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Refine LS restraints |
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LS refinement shell |
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