+Open data
-Basic information
Entry | Database: PDB / ID: 1ol6 | ||||||
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Title | Structure of unphosphorylated D274N mutant of Aurora-A | ||||||
Components | SERINE/THREONINE KINASE 6 | ||||||
Keywords | TRANSFERASE / CELL CYCLE / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / PHOSPHORYLATION | ||||||
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 / 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 / regulation of G2/M transition of mitotic cell cycle / SUMOylation of DNA replication proteins / spindle midzone / centriole / protein serine/threonine/tyrosine kinase activity / liver regeneration / 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 / 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 / G2/M transition of mitotic cell cycle / response to wounding / spindle / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / mitotic cell cycle / peptidyl-serine phosphorylation / basolateral plasma membrane / midbody / Regulation of TP53 Activity through Phosphorylation / proteasome-mediated ubiquitin-dependent protein catabolic process / protein autophosphorylation / microtubule / postsynaptic density / non-specific serine/threonine protein kinase / protein kinase activity / protein heterodimerization activity / protein phosphorylation / cell division / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / ubiquitin protein ligase binding / glutamatergic synapse / negative regulation of apoptotic process / protein kinase binding / apoptotic process / perinuclear region of cytoplasm / nucleoplasm / ATP binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3 Å | ||||||
Authors | Bayliss, R. / Conti, E. | ||||||
Citation | Journal: Mol.Cell / Year: 2003 Title: Structural Basis of Aurora-A Activation by Tpx2 at the Mitotic Spindle. Authors: Bayliss, R. / Sardon, T. / Vernos, I. / Conti, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ol6.cif.gz | 63 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ol6.ent.gz | 43.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ol6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ol6_validation.pdf.gz | 713.6 KB | Display | wwPDB validaton report |
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Full document | 1ol6_full_validation.pdf.gz | 719.4 KB | Display | |
Data in XML | 1ol6_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | 1ol6_validation.cif.gz | 15.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ol/1ol6 ftp://data.pdbj.org/pub/pdb/validation_reports/ol/1ol6 | HTTPS FTP |
-Related structure data
Related structure data | 1ol5C 1ol7C 1fotS 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: 32688.471 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 122-403 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): CODONPLUS RIL / References: UniProt: O14965, EC: 2.7.1.37 |
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#2: Chemical | ChemComp-ATP / |
#3: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.43 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.3 Details: 20% PEG3350, 190 MM NACL, 10 MM NAH2PO4, 100 MM TRIS PH 7.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.91839 |
Detector | Date: Mar 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91839 Å / Relative weight: 1 |
Reflection | Resolution: 3→58 Å / Num. obs: 12265 / % possible obs: 98.4 % / Redundancy: 7.1 % / Rmerge(I) obs: 0.165 / Net I/σ(I): 3.6 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 7.5 % / Rmerge(I) obs: 0.432 / Mean I/σ(I) obs: 1.5 / % possible all: 98.4 |
-Processing
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Refinement | Method to determine structure: MAD Starting model: PDB ENTRY 1FOT Resolution: 3→40 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3→40 Å
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Refine LS restraints |
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