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Yorodumi- PDB-1ipi: CRYSTAL STRUCTURE OF THE ARCHAEAL HOLLIDAY JUNCTION RESOLVASE HJC... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1ipi | ||||||
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| Title | CRYSTAL STRUCTURE OF THE ARCHAEAL HOLLIDAY JUNCTION RESOLVASE HJC FROM PYROCOCCUS FURIOSUS FORM II | ||||||
Components | HOLLIDAY JUNCTION RESOLVASE | ||||||
Keywords | HYDROLASE / nuclease fold / HJC | ||||||
| Function / homology | Function and homology informationcrossover junction endodeoxyribonuclease / Holliday junction resolvase complex / crossover junction DNA endonuclease activity / DNA recombination / DNA repair / magnesium ion binding / DNA binding Similarity search - Function | ||||||
| Biological species | ![]() Pyrococcus furiosus (archaea) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.16 Å | ||||||
Authors | Nishino, T. / Komori, K. / Ishino, Y. / Morikawa, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001Title: Dissection of the regional roles of the archaeal Holliday junction resolvase Hjc by structural and mutational analyses. Authors: Nishino, T. / Komori, K. / Ishino, Y. / Morikawa, K. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1ipi.cif.gz | 59.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1ipi.ent.gz | 43.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1ipi.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1ipi_validation.pdf.gz | 433.5 KB | Display | wwPDB validaton report |
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| Full document | 1ipi_full_validation.pdf.gz | 438.9 KB | Display | |
| Data in XML | 1ipi_validation.xml.gz | 12.8 KB | Display | |
| Data in CIF | 1ipi_validation.cif.gz | 17.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ip/1ipi ftp://data.pdbj.org/pub/pdb/validation_reports/ip/1ipi | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1gefS S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Details | chain A and B form functional dimer |
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Components
| #1: Protein | Mass: 13792.379 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Pyrococcus furiosus (archaea) / Gene: HJC / Plasmid: PET21 / Species (production host): Escherichia coli / Production host: ![]() References: UniProt: Q9V301, UniProt: E7FHX4*PLUS, crossover junction endodeoxyribonuclease #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: 2.53 Å3/Da / Density % sol: 51.41 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 297 K / Method: vapor diffusion / pH: 7 Details: 100mM Tris-HCl, 1mM EDTA, 32.5% PEG4000, 10% glycerol , pH 7.0, VAPOR DIFFUSION, temperature 297K | ||||||||||||||||||||||||||||||||||||
| Crystal grow | *PLUS Temperature: 20 ℃ / Method: batch method | ||||||||||||||||||||||||||||||||||||
| 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: SPring-8 / Beamline: BL24XU / Wavelength: 0.834 Å |
| Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Dec 11, 2000 |
| Radiation | Monochromator: DIAMOND / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.834 Å / Relative weight: 1 |
| Reflection | Resolution: 2.15→41.1 Å / Num. all: 94745 / Num. obs: 13043 / % possible obs: 88.9 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 7.3 % / Biso Wilson estimate: 37 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 6.42 |
| Reflection shell | Resolution: 2.16→2.26 Å / Redundancy: 6 % / Rmerge(I) obs: 0.279 / Mean I/σ(I) obs: 2.7 / % possible all: 79.5 |
| Reflection | *PLUS Highest resolution: 2.16 Å / Lowest resolution: 41 Å / Rmerge(I) obs: 0.064 |
| Reflection shell | *PLUS Lowest resolution: 2.27 Å / % possible obs: 79.5 % |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1GEF functional dimer Resolution: 2.16→41 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 2.16→41 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.16→2.24 Å
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| Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
| Refinement | *PLUS Lowest resolution: 41 Å / Num. reflection obs: 13043 / % reflection Rfree: 11.48 % / Rfactor obs: 0.214 | |||||||||||||||||||||||||
| Solvent computation | *PLUS | |||||||||||||||||||||||||
| Displacement parameters | *PLUS | |||||||||||||||||||||||||
| Refine LS restraints | *PLUS
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| LS refinement shell | *PLUS Lowest resolution: 2.27 Å / Rfactor Rfree: 0.307 / Rfactor Rwork: 0.233 / Rfactor obs: 0.233 |
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Pyrococcus furiosus (archaea)
X-RAY DIFFRACTION
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