+Open data
-Basic information
Entry | Database: PDB / ID: 4a1z | ||||||
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Title | Eg5-1 | ||||||
Components | KINESIN-LIKE PROTEIN KIF11 | ||||||
Keywords | MOTOR PROTEIN | ||||||
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 / spindle microtubule / 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: 2.8 Å | ||||||
Authors | Talapatra, S.K. / Kozielski, F. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2013 Title: The Mitotic Kinesin Eg5 Overcomes Inhibition to the Phase I/II Clinical Candidate Sb743921 by an Allosteric Resistance Mechanism. Authors: Talapatra, S.K. / Anthony, N.G. / Mackay, S.P. / Kozielski, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4a1z.cif.gz | 144.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4a1z.ent.gz | 111.6 KB | Display | PDB format |
PDBx/mmJSON format | 4a1z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4a1z_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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Full document | 4a1z_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 4a1z_validation.xml.gz | 28.1 KB | Display | |
Data in CIF | 4a1z_validation.cif.gz | 39 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/4a1z ftp://data.pdbj.org/pub/pdb/validation_reports/a1/4a1z | HTTPS FTP |
-Related structure data
Related structure data | 4a28C 4as7C 4b7bC 4bxnC 1ii6S S: Starting model for refinement C: citing same article (ref.) |
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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
#1: Protein | Mass: 41039.625 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P52732 #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 42.35 % / Description: NONE |
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Crystal grow | pH: 6.8 / Details: 14% PEG 3350 0.2 M NA NO3 0.1 M MES (PH 5.6). |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9763 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 18414 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 3.3 % / Biso Wilson estimate: 26.37 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 12.7 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 4.6 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1II6 Resolution: 2.8→29.232 Å / SU ML: 0.36 / σ(F): 0 / Phase error: 24.94 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 27.476 Å2 / ksol: 0.345 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.14 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→29.232 Å
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Refine LS restraints |
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LS refinement shell |
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