+Open data
-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 information bacterial-type DNA replication / recombinational repair / 3'-5' DNA helicase activity / DNA unwinding involved in DNA replication / 3'-5' exonuclease activity / DNA helicase activity / response to radiation / single-stranded DNA binding / DNA helicase / DNA repair ...bacterial-type DNA replication / recombinational repair / 3'-5' DNA helicase activity / DNA unwinding involved in DNA replication / 3'-5' exonuclease activity / DNA helicase activity / response to radiation / single-stranded DNA binding / DNA helicase / DNA repair / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å | ||||||
Authors | Korolev, S. / Waksman, G. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1997 Title: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-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
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ua/1uaa ftp://data.pdbj.org/pub/pdb/validation_reports/ua/1uaa | 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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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.) Escherichia coli (E. coli) |
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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 |
-Processing
Software |
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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 |