+Open data
-Basic information
Entry | Database: PDB / ID: 4ubf | ||||||
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Title | HsMCAK motor domain complex | ||||||
Components | (Kinesin-like protein KIF2C) x 2 | ||||||
Keywords | CELL CYCLE / MCAK / Kif2c / Complex / Motor domain | ||||||
Function / homology | Function and homology information regulation of chromosome segregation / metaphase chromosome alignment / establishment or maintenance of microtubule cytoskeleton polarity / centromeric DNA binding / microtubule plus-end / attachment of mitotic spindle microtubules to kinetochore / microtubule plus-end binding / Kinesins / COPI-dependent Golgi-to-ER retrograde traffic / microtubule depolymerization ...regulation of chromosome segregation / metaphase chromosome alignment / establishment or maintenance of microtubule cytoskeleton polarity / centromeric DNA binding / microtubule plus-end / attachment of mitotic spindle microtubules to kinetochore / microtubule plus-end binding / Kinesins / COPI-dependent Golgi-to-ER retrograde traffic / microtubule depolymerization / kinesin complex / microtubule motor activity / mitotic metaphase chromosome alignment / microtubule-based movement / chromosome, centromeric region / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / MHC class II antigen presentation / RHO GTPases Activate Formins / spindle / kinetochore / Separation of Sister Chromatids / microtubule cytoskeleton / microtubule binding / microtubule / cell division / centrosome / ATP hydrolysis activity / ATP binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Welburn, J.P.I. / Talapatra, S.K. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Elife / Year: 2015 Title: The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch. Authors: Talapatra, S.K. / Harker, B. / Welburn, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ubf.cif.gz | 264.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ubf.ent.gz | 206.1 KB | Display | PDB format |
PDBx/mmJSON format | 4ubf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ub/4ubf ftp://data.pdbj.org/pub/pdb/validation_reports/ub/4ubf | HTTPS FTP |
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-Related structure data
Related structure data | 2hehS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 43295.602 Da / Num. of mol.: 4 / Fragment: UNP Residues 225-593 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIF2C, KNSL6 / Details (production host): pET28a-LIC / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q99661 #2: Protein/peptide | | Mass: 1376.450 Da / Num. of mol.: 1 / Fragment: UNP Residues 709-720 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIF2C, KNSL6 / Plasmid: pET28a-LIC / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q99661 #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-ADP / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.94 % / Description: Single Rectangular Crystal |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6.8 Details: 24 % w/v PEG 1500 20 % v/v Glycerol Protein crystals appeared after two days and single crystals were used for measurement Temp details: Controlled Temperature Room |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.987 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Jul 11, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. all: 155983 / Num. obs: 35146 / % possible obs: 99.8 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.091 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 3→3.5 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.682 / Mean I/σ(I) obs: 2 / % possible all: 100 |
-Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.8.2_1309) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2HEH Resolution: 3→29.492 Å / SU ML: 0.52 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.46 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→29.492 Å
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Refine LS restraints |
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LS refinement shell |
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