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- PDB-3euk: Crystal structure of MukE-MukF(residues 292-443)-MukB(head domain... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3euk | ||||||
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Title | Crystal structure of MukE-MukF(residues 292-443)-MukB(head domain)-ATPgammaS complex, asymmetric dimer | ||||||
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![]() | CELL CYCLE / MukB / MukE / MukF / Chromosome condensation / condensin / SMC / non-SMC subunit / ABC-type ATPase / WHD / ATP-binding / Cell division / Chromosome partition / DNA condensation / DNA-binding / Nucleotide-binding | ||||||
Function / homology | ![]() nucleoid / chromosome condensation / chromosome segregation / DNA replication / cell cycle / cell division / calcium ion binding / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Woo, J.S. / Lim, J.H. / Shin, H.C. / Oh, B.H. | ||||||
![]() | ![]() Title: Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions. Authors: Woo, J.S. / Lim, J.H. / Shin, H.C. / Suh, M.K. / Ku, B. / Lee, K.H. / Joo, K. / Robinson, H. / Lee, J. / Park, S.Y. / Ha, N.C. / Oh, B.H. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 466.6 KB | Display | ![]() |
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PDB format | ![]() | 374.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 102.3 KB | Display | |
Data in CIF | ![]() | 134.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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: 54102.809 Da / Num. of mol.: 4 / Fragment: Head domain / Mutation: E1435Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: mukB, HD_1582 / Plasmid: pPROEX / Production host: ![]() ![]() #2: Protein | Mass: 17334.508 Da / Num. of mol.: 2 / Fragment: residues 292-443 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Protein | Mass: 26815.508 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #4: Chemical | ChemComp-AGS / #5: Chemical | ChemComp-MG / Sequence details | THESE RESIDUES ARE NATURAL GENETIC VARIANTS, POLYMORPHI | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 64.46 % / Mosaicity: 0.412 ° |
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Crystal grow | Temperature: 296 K / Method: hanging drop / pH: 8 Details: PEG 10000, MgCl2, pH 8.0, hanging drop, temperature 296K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 9, 2007 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 4→30 Å / Num. obs: 34959 / % possible obs: 92.8 % / Redundancy: 6 % / Rmerge(I) obs: 0.077 / Χ2: 0.84 / Net I/σ(I): 11.576 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Resolution: 4→20 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.756 / σ(F): 0
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Solvent computation | Bsol: 35.472 Å2 | ||||||||||||||||||||
Displacement parameters | Biso max: 200 Å2 / Biso mean: 130.265 Å2 / Biso min: 26.49 Å2
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Refinement step | Cycle: LAST / Resolution: 4→20 Å
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Refine LS restraints |
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Xplor file |
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