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Yorodumi- PDB-1ol5: Structure of Aurora-A 122-403, phosphorylated on Thr287, Thr288 a... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ol5 | ||||||
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Title | Structure of Aurora-A 122-403, phosphorylated on Thr287, Thr288 and bound to TPX2 1-43 | ||||||
Components |
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Keywords | TRANSFERASE/CELL CYCLE / TRANSFERASE-CELL CYCLE COMPLEX / CELL CYCLE / TRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / PHOSPHORYLATION | ||||||
Function / homology | Function and homology information Interaction between PHLDA1 and AURKA / microtubule nucleation / regulation of centrosome cycle / negative regulation of microtubule depolymerization / axon hillock / importin-alpha family protein binding / spindle assembly involved in female meiosis I / cilium disassembly / positive regulation of oocyte maturation / spindle pole centrosome ...Interaction between PHLDA1 and AURKA / microtubule nucleation / regulation of centrosome cycle / negative regulation of microtubule depolymerization / axon hillock / importin-alpha family protein binding / 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 / intercellular bridge / positive regulation of mitochondrial fission / activation of protein kinase activity / mitotic spindle pole / regulation of G2/M transition of mitotic cell cycle / SUMOylation of DNA replication proteins / mitotic spindle assembly / spindle midzone / regulation of mitotic spindle organization / 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 / spindle pole / 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 / molecular adaptor activity / 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: 2.5 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 | 1ol5.cif.gz | 80.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ol5.ent.gz | 58.6 KB | Display | PDB format |
PDBx/mmJSON format | 1ol5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ol5_validation.pdf.gz | 804.3 KB | Display | wwPDB validaton report |
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Full document | 1ol5_full_validation.pdf.gz | 809.3 KB | Display | |
Data in XML | 1ol5_validation.xml.gz | 15.7 KB | Display | |
Data in CIF | 1ol5_validation.cif.gz | 21.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ol/1ol5 ftp://data.pdbj.org/pub/pdb/validation_reports/ol/1ol5 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 |
-Components
-Protein / Protein/peptide , 2 types, 2 molecules AB
#1: Protein | Mass: 32849.418 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 122-403 Source method: isolated from a genetically manipulated source Details: PHOSPHORYLATED ON THR287, THR288 / 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: Protein/peptide | Mass: 4911.110 Da / Num. of mol.: 1 / Fragment: N-TERMINAL, RESIDUES 1-43 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: Q9ULW0 |
-Non-polymers , 4 types, 151 molecules
#3: Chemical | ChemComp-ADP / | ||||
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#4: Chemical | #5: Chemical | #6: 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: 2.8 Å3/Da / Density % sol: 55.3 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: 18% (W/V) PEG8000, 100 MM MES PH 6.5, 200 MM MGSO4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1 |
Detector | Date: Apr 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→40 Å / Num. obs: 14609 / % possible obs: 100 % / Observed criterion σ(I): 6 / Redundancy: 5.6 % / Rmerge(I) obs: 0.099 / Net I/σ(I): 5.1 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.248 / Mean I/σ(I) obs: 1.1 / % possible all: 100 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 40 Å / % possible obs: 100 % / Redundancy: 5.6 % / Rmerge(I) obs: 0.099 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / % possible obs: 100 % / Redundancy: 5.7 % / Rmerge(I) obs: 0.248 / Mean I/σ(I) obs: 1.1 |
-Processing
Software |
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Refinement | Method to determine structure: MAD Starting model: UNPHOSPHORYLATED AURORA/TPX2 Resolution: 2.5→40 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.5→40 Å
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Refine LS restraints |
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Refinement | *PLUS % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |