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Open data
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Basic information
| Entry | Database: PDB / ID: 1uaa | ||||||
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| Title | E. COLI REP HELICASE/DNA COMPLEX | ||||||
Components |
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Keywords | HYDROLASE/DNA / COMPLEX (HELICASE-DNA) / HELICASE / DNA UNWINDING / HYDROLASE-DNA COMPLEX | ||||||
| Function / homology | Function and homology informationcytoplasmic replisome / DnaB-DnaC-Rep-PriC complex / bacterial-type DNA replication / primosome complex / DNA replication, synthesis of primer / recombinational repair / DNA 3'-5' helicase / 3'-5' DNA helicase activity / replication fork processing / DNA helicase activity ...cytoplasmic replisome / DnaB-DnaC-Rep-PriC complex / bacterial-type DNA replication / primosome complex / DNA replication, synthesis of primer / recombinational repair / DNA 3'-5' helicase / 3'-5' DNA helicase activity / replication fork processing / DNA helicase activity / response to radiation / single-stranded DNA binding / protein homodimerization activity / ATP hydrolysis activity / ATP binding / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å | ||||||
Authors | Korolev, S. / Waksman, G. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1997Title: Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Authors: Korolev, S. / Hsieh, J. / Gauss, G.H. / Lohman, T.M. / Waksman, G. | ||||||
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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 | 1uaa.cif.gz | 262.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1uaa.ent.gz | 212.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1uaa.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1uaa_validation.pdf.gz | 394 KB | Display | wwPDB validaton report |
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| Full document | 1uaa_full_validation.pdf.gz | 520.7 KB | Display | |
| Data in XML | 1uaa_validation.xml.gz | 42.6 KB | Display | |
| Data in CIF | 1uaa_validation.cif.gz | 62.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ua/1uaa ftp://data.pdbj.org/pub/pdb/validation_reports/ua/1uaa | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: DNA chain | Mass: 4822.127 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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| #2: Protein | Mass: 77042.078 Da / Num. of mol.: 2 / Source method: obtained synthetically References: UniProt: P09980, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 4.5 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 8 / Details: pH 8.00, VAPOR DIFFUSION, temperature 293.00K | ||||||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions |
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| Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
| Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8 / 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: SSRL / Beamline: BL7-1 |
| Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 7, 1996 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Relative weight: 1 |
| Reflection | Resolution: 3→30 Å / Num. obs: 57472 / % possible obs: 97.3 % / Redundancy: 7 % / Rmerge(I) obs: 0.053 |
| Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 30 Å / % possible obs: 97.3 % / Num. measured all: 434546 |
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Processing
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| Refinement | Resolution: 3→15 Å / σ(F): 2
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| Displacement parameters | Biso mean: 41 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3→15 Å
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| Refine LS restraints |
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| Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 15 Å / σ(I): 2 / Rfactor all: 0.235 / Rfactor obs: 0.228 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS Biso mean: 41 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.918 |
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