+Open data
-Basic information
Entry | Database: PDB / ID: 4bn1 | ||||||
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Title | Crystal structure of V174M mutant of Aurora-A kinase | ||||||
Components | AURORA KINASE A | ||||||
Keywords | TRANSFERASE / PROTEIN KINASE / MITOSIS | ||||||
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 cytokinesis / regulation of signal transduction by p53 class mediator / 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 / protein serine/threonine kinase activity / centrosome / 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: 2.499 Å | ||||||
Authors | Bibby, R.A. / Bayliss, R. | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2013 Title: Insights Into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification. Authors: Rowan, F.C. / Richards, M. / Bibby, R.A. / Thompson, A. / Bayliss, R. / Blagg, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4bn1.cif.gz | 72.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4bn1.ent.gz | 51.5 KB | Display | PDB format |
PDBx/mmJSON format | 4bn1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bn/4bn1 ftp://data.pdbj.org/pub/pdb/validation_reports/bn/4bn1 | HTTPS FTP |
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-Related structure data
Related structure data | 1ol7S 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 33140.809 Da / Num. of mol.: 1 / Fragment: 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) References: UniProt: O14965, non-specific serine/threonine protein kinase | ||||
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#2: Chemical | ChemComp-ADP / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | N-TERMINAL GLY-ALA FROM VECTOR SEQUENCE | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.65 % / Description: NONE |
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Crystal grow | Details: 0.1 M HEPES PH 7.5, 10 % PEG 6000, 5 % MPD AND 0.1 M CALCIUM CHLORIDE DIHYDRATE |
-Data collection
Diffraction | Mean temperature: 92 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9721 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9721 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→70.71 Å / Num. obs: 140297 / % possible obs: 100 % / Observed criterion σ(I): 6 / Redundancy: 11.1 % / Biso Wilson estimate: 54.75 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 10.3 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 3.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1OL7 Resolution: 2.499→65.557 Å / SU ML: 0.26 / σ(F): 1.38 / Phase error: 24.18 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.236 Å2 / ksol: 0.349 e/Å3 | |||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.76 Å2
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Refinement step | Cycle: LAST / Resolution: 2.499→65.557 Å
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Refine LS restraints |
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LS refinement shell |
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