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Yorodumi- PDB-1ii6: Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP. -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ii6 | ||||||
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Title | Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP. | ||||||
Components | KINESIN-RELATED MOTOR PROTEIN Eg5 | ||||||
Keywords | CELL CYCLE / Mg-ADP complex | ||||||
Function / homology | Function and homology information spindle elongation / regulation of mitotic centrosome separation / Kinesins / plus-end-directed microtubule motor activity / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / microtubule motor activity / kinesin complex / spindle organization / microtubule-based movement ...spindle elongation / regulation of mitotic centrosome separation / Kinesins / plus-end-directed microtubule motor activity / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / microtubule motor activity / kinesin complex / spindle organization / microtubule-based movement / mitotic spindle assembly / MHC class II antigen presentation / mitotic spindle organization / mitotic spindle / spindle pole / spindle / 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 / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Turner, J. / Anderson, R. / Guo, J. / Beraud, C. / Sakowicz, R. / Fletterick, R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. Authors: Turner, J. / Anderson, R. / Guo, J. / Beraud, C. / Fletterick, R. / Sakowicz, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ii6.cif.gz | 152.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ii6.ent.gz | 120.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ii6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ii6_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 1ii6_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 1ii6_validation.xml.gz | 32.5 KB | Display | |
Data in CIF | 1ii6_validation.cif.gz | 45.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ii/1ii6 ftp://data.pdbj.org/pub/pdb/validation_reports/ii/1ii6 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 41055.582 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-368 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: Eg5 / Plasmid: pET 43d / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Bl21 (DE3) / References: UniProt: P52732 #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.44 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: PEG 3350, MES, socium nitrate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.8 / Details: used seeding | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 | ||||||||||||||||||||||||
Reflection | Resolution: 2.1→50 Å / Num. all: 236822 / Num. obs: 42896 / % possible obs: 94.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.5 % / Rmerge(I) obs: 0.125 / Net I/σ(I): 9.4 | ||||||||||||||||||||||||
Reflection shell | Resolution: 2.1→2.14 Å / Rmerge(I) obs: 0.103 / Num. unique all: 1924 / % possible all: 85 | ||||||||||||||||||||||||
Reflection | *PLUS Num. measured all: 236822 | ||||||||||||||||||||||||
Reflection shell | *PLUS % possible obs: 85 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: catalytic core of KAR3 Resolution: 2.1→50 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 50 Å / σ(F): 2 / Rfactor obs: 0.2178 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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