+Open data
-Basic information
Entry | Database: PDB / ID: 4zhi | ||||||
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Title | Eg5 motor domain mutant E162S | ||||||
Components | Kinesin-like protein KIF11 | ||||||
Keywords | MOTOR PROTEIN / 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. / Park, C. / Worthylake, D. / Kim, S. | ||||||
Citation | Journal: To Be Published Title: Eg5 Authors: Richard, J. / Kim, E. / Luo, M. / Worthylake, D. / Wojcik, E. / Kim, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4zhi.cif.gz | 149 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4zhi.ent.gz | 115.8 KB | Display | PDB format |
PDBx/mmJSON format | 4zhi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zh/4zhi ftp://data.pdbj.org/pub/pdb/validation_reports/zh/4zhi | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 41126.703 Da / Num. of mol.: 2 / Mutation: E162S 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) / References: UniProt: P52732 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.63 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: 200 mM NaF and 18-20% PEG 3350 |
-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 10, 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: 30404 / % possible obs: 98.1 % / Redundancy: 1.85 % / Rmerge(I) obs: 0.0673 / Net I/σ(I): 8.45 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 1.45 % / Rmerge(I) obs: 0.2559 / Mean I/σ(I) obs: 2.77 / % possible all: 96.6 |
-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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