+Open data
-Basic information
Entry | Database: PDB / ID: 2cvf | ||||||
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Title | Crystal structure of the RadB recombinase | ||||||
Components | DNA repair and recombination protein radB | ||||||
Keywords | DNA BINDING PROTEIN / RadB / filament formation / homologous recombination / ATPase domain / hyperthermophile | ||||||
Function / homology | Function and homology information ATP-dependent DNA damage sensor activity / DNA recombination / damaged DNA binding / DNA repair / ATP binding Similarity search - Function | ||||||
Biological species | Thermococcus kodakarensis (archaea) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.6 Å | ||||||
Authors | Akiba, T. / Ishii, N. / Rashid, N. / Morikawa, M. / Imanaka, T. / Harata, K. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2005 Title: Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly Authors: Akiba, T. / Ishii, N. / Rashid, N. / Morikawa, M. / Imanaka, T. / Harata, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2cvf.cif.gz | 102.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2cvf.ent.gz | 78.9 KB | Display | PDB format |
PDBx/mmJSON format | 2cvf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2cvf_validation.pdf.gz | 434 KB | Display | wwPDB validaton report |
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Full document | 2cvf_full_validation.pdf.gz | 484.6 KB | Display | |
Data in XML | 2cvf_validation.xml.gz | 27 KB | Display | |
Data in CIF | 2cvf_validation.cif.gz | 37.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cv/2cvf ftp://data.pdbj.org/pub/pdb/validation_reports/cv/2cvf | HTTPS FTP |
-Related structure data
-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: 24578.344 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermococcus kodakarensis (archaea) / Gene: Pk-REC / Plasmid: pET-8c / Production host: Escherichia coli (E. coli) / Strain (production host): HMS174(DE)pLysS / References: UniProt: P95547 #2: 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: 2.2 Å3/Da / Density % sol: 42.8 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 0.2M ammonium sulphate, 30% polyethylene glycol monomethyl ether 2000, 0.1M acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ROTATING ANODE / Type: MACSCIENCE / Wavelength: 1.5418 Å |
Detector | Type: BRUKER SMART 6000 / Detector: CCD / Date: May 11, 2002 / Details: Osmic Confocal Max-Flux optics |
Radiation | Monochromator: Osmic Confocal Max-Flux optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→24.7 Å / Num. obs: 16828 / % possible obs: 99.5 % / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.4→2.53 Å / % possible all: 98.7 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.6→6 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.6→6 Å
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