+Open data
-Basic information
Entry | Database: PDB / ID: 4zca | ||||||
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Title | Eg5 motor domain mutant Y231F | ||||||
Components | Kinesin-like protein KIF11 | ||||||
Keywords | MOTOR PROTEIN / Kinesin / mitosis / ATPase | ||||||
Function / homology | Function and homology information spindle elongation / Kinesins / plus-end-directed microtubule motor activity / regulation of mitotic centrosome separation / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / microtubule motor activity / spindle organization / microtubule-based movement ...spindle elongation / Kinesins / plus-end-directed microtubule motor activity / regulation of mitotic centrosome separation / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / microtubule motor activity / spindle organization / microtubule-based movement / mitotic spindle assembly / MHC class II antigen presentation / mitotic spindle organization / mitotic spindle / spindle / spindle pole / mitotic cell cycle / microtubule binding / microtubule / cell division / protein kinase binding / protein-containing complex / ATP binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Luo, M. / Parke, C. / Worthylake, D. | ||||||
Citation | Journal: To Be Published Title: Eg5 Authors: Richard, J. / Kim, E. / Luo, M. / Wojcik, E. / Worthylake, D. / Kim, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4zca.cif.gz | 145.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4zca.ent.gz | 114.2 KB | Display | PDB format |
PDBx/mmJSON format | 4zca.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zc/4zca ftp://data.pdbj.org/pub/pdb/validation_reports/zc/4zca | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 41152.738 Da / Num. of mol.: 2 / Mutation: Y231F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIF11, EG5, KNSL1, TRIP5 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P52732 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.7 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 200 mM NaNO3, 20-25% PEG 3350, 100 mM MES pH 5.5-5.7, 5-10% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.5418 Å |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Apr 7, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→25 Å / Num. obs: 32744 / % possible obs: 98.2 % / Redundancy: 4.54 % / Rmerge(I) obs: 0.1161 / Net I/σ(I): 8.49 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 2.62 % / Rmerge(I) obs: 0.3752 / Mean I/σ(I) obs: 1.91 / % possible all: 97.8 |
-Processing
Software |
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Refinement | Resolution: 2.3→25 Å
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Refinement step | Cycle: LAST / Resolution: 2.3→25 Å
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