+Open data
-Basic information
Entry | Database: PDB / ID: 3kta | ||||||
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Title | Structural Basis for Adenylate Kinase Activity in ABC ATPases | ||||||
Components | (Chromosome segregation protein smc) x 2 | ||||||
Keywords | TRANSFERASE / structural maintenance of chromosomes / SMC / ABC ATPase / CFTR / adenylate kinase / AP5A | ||||||
Function / homology | Function and homology information chromosome condensation / sister chromatid cohesion / chromosome segregation / chromosome / DNA replication / ATP hydrolysis activity / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.627 Å | ||||||
Authors | Lammens, A. / Hopfner, K.P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2010 Title: Structural Basis for Adenylate Kinase Activity in ABC ATPases. Authors: Lammens, A. / Hopfner, K.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3kta.cif.gz | 157.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3kta.ent.gz | 130.8 KB | Display | PDB format |
PDBx/mmJSON format | 3kta.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kt/3kta ftp://data.pdbj.org/pub/pdb/validation_reports/kt/3kta | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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: 20416.777 Da / Num. of mol.: 2 / Fragment: residues 115-296 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Gene: PF1843 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8TZY2 #2: Protein | Mass: 19635.633 Da / Num. of mol.: 2 / Fragment: residues 1120-1291 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Gene: PF1843 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8TZY2 #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.82 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.6 Details: BisTRIS, 16% PEG3350, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 26, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→50 Å / Num. obs: 84052 / % possible obs: 95.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.6→1.6455 Å / % possible all: 95.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.627→35.435 Å / SU ML: 0.19 / σ(F): 1.37 / Phase error: 20.07 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 50.158 Å2 / ksol: 0.35 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.627→35.435 Å
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Refine LS restraints |
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LS refinement shell |
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