+Open data
-Basic information
Entry | Database: PDB / ID: 1w36 | ||||||
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Title | RecBCD:DNA complex | ||||||
Components |
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Keywords | RECOMBINATION / HELICASE / NUCLEASE / HYDROLASE / DNA REPAIR | ||||||
Function / homology | Function and homology information exodeoxyribonuclease V / exodeoxyribonuclease V activity / exodeoxyribonuclease V complex / DNA 5'-3' helicase / clearance of foreign intracellular DNA / DNA 3'-5' helicase / DNA translocase activity / single-stranded DNA helicase activity / recombinational repair / 3'-5' DNA helicase activity ...exodeoxyribonuclease V / exodeoxyribonuclease V activity / exodeoxyribonuclease V complex / DNA 5'-3' helicase / clearance of foreign intracellular DNA / DNA 3'-5' helicase / DNA translocase activity / single-stranded DNA helicase activity / recombinational repair / 3'-5' DNA helicase activity / ATP-dependent activity, acting on DNA / DNA helicase activity / DNA endonuclease activity / helicase activity / double-strand break repair via homologous recombination / response to radiation / DNA recombination / DNA damage response / magnesium ion binding / ATP hydrolysis activity / DNA binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 3.1 Å | ||||||
Authors | Singleton, M.R. / Dillingham, M.S. / Gaudier, M. / C Kowalczykowski, S. / Wigley, D.B. | ||||||
Citation | Journal: Nature / Year: 2004 Title: Crystal Structure of Recbcd Enzyme Reveals a Machine for Processing DNA Breaks Authors: Singleton, M.R. / Dillingham, M.S. / Gaudier, M. / Kowalczykowski, S.C. / Wigley, D.B. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1w36.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1w36.ent.gz | 944.2 KB | Display | PDB format |
PDBx/mmJSON format | 1w36.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w3/1w36 ftp://data.pdbj.org/pub/pdb/validation_reports/w3/1w36 | 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: 134110.641 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P08394, exodeoxyribonuclease V #2: Protein | Mass: 128974.102 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P07648, exodeoxyribonuclease V #3: Protein | Mass: 66990.367 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P04993, exodeoxyribonuclease V #4: DNA chain | Mass: 13170.455 Da / Num. of mol.: 2 / Source method: obtained synthetically #5: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.53 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→46.8 Å / Num. obs: 151577 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 17.8 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 3.1→46.84 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 4860428.14 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 68.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→46.84 Å
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Refine LS restraints |
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