+Open data
-Basic information
Entry | Database: PDB / ID: 1a0p | ||||||
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Title | SITE-SPECIFIC RECOMBINASE, XERD | ||||||
Components | SITE-SPECIFIC RECOMBINASE XERD | ||||||
Keywords | DNA RECOMBINATION / XERD / RECOMBINASE / DNA BINDING | ||||||
Function / homology | Function and homology information tyrosine-based site-specific recombinase activity / site-specific recombinase activity / resolution of DNA recombination intermediates / DNA transposition / Holliday junction resolvase complex / plasmid maintenance / cell cycle / chromosome segregation / response to radiation / cell division ...tyrosine-based site-specific recombinase activity / site-specific recombinase activity / resolution of DNA recombination intermediates / DNA transposition / Holliday junction resolvase complex / plasmid maintenance / cell cycle / chromosome segregation / response to radiation / cell division / DNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.5 Å | ||||||
Authors | Subramanya, H.S. / Arciszewska, L.K. / Baker, R.A. / Bird, L.E. / Sherratt, D.J. / Wigley, D.B. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Crystal structure of the site-specific recombinase, XerD. Authors: Subramanya, H.S. / Arciszewska, L.K. / Baker, R.A. / Bird, L.E. / Sherratt, D.J. / Wigley, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a0p.cif.gz | 69 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a0p.ent.gz | 51.6 KB | Display | PDB format |
PDBx/mmJSON format | 1a0p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a0p_validation.pdf.gz | 426.9 KB | Display | wwPDB validaton report |
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Full document | 1a0p_full_validation.pdf.gz | 445.9 KB | Display | |
Data in XML | 1a0p_validation.xml.gz | 15.3 KB | Display | |
Data in CIF | 1a0p_validation.cif.gz | 20.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a0/1a0p ftp://data.pdbj.org/pub/pdb/validation_reports/a0/1a0p | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 33308.191 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cell line: 293 / Production host: Escherichia coli (E. coli) / Strain (production host): DS9009 / References: UniProt: P0A8P8 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.08 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→15 Å / Num. obs: 11671 / % possible obs: 98.9 % / Redundancy: 3 % / Rsym value: 0.048 |
Reflection shell | Resolution: 2.5→2.59 Å / Rsym value: 0.19 / % possible all: 99.9 |
Reflection | *PLUS Rmerge(I) obs: 0.048 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.5→10 Å
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.224 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |