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Open data
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Basic information
Entry | Database: PDB / ID: 1qhh | ||||||
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Title | STRUCTURE OF DNA HELICASE WITH ADPNP | ||||||
![]() | (PROTEIN (PCRA ...) x 4 | ||||||
![]() | HYDROLASE / DNA REPAIR / DNA REPLICATION / SOS RESPONSE / HELICASE / ATP-BINDING / DNA-BINDING | ||||||
Function / homology | ![]() DNA helicase complex / DNA 3'-5' helicase / recombinational repair / DNA unwinding involved in DNA replication / 3'-5' DNA helicase activity / isomerase activity / ATP hydrolysis activity / DNA binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Soultanas, P. / Dillingham, M.S. / Velankar, S.S. / Wigley, D.B. | ||||||
![]() | ![]() Title: DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. Authors: Soultanas, P. / Dillingham, M.S. / Velankar, S.S. / Wigley, D.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.6 KB | Display | ![]() |
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PDB format | ![]() | 112.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 919.9 KB | Display | ![]() |
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Full document | ![]() | 938.9 KB | Display | |
Data in XML | ![]() | 26.8 KB | Display | |
Data in CIF | ![]() | 36.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
-PROTEIN (PCRA ... , 4 types, 4 molecules ABCD
#1: Protein | Mass: 18850.926 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: NCA1503 / Gene: PCRA / Plasmid: PET22 / Gene (production host): PCRA / Production host: ![]() ![]() |
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#2: Protein | Mass: 32419.732 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: NCA1503 / Gene: PCRA / Plasmid: PET22 / Gene (production host): PCRA / Production host: ![]() ![]() |
#3: Protein | Mass: 12821.245 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: NCA1503 / Gene: PCRA / Plasmid: PET22 / Gene (production host): PCRA / Production host: ![]() ![]() |
#4: Protein | Mass: 18557.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: NCA1503 / Gene: PCRA / Plasmid: PET22 / Gene (production host): PCRA / Production host: ![]() ![]() |
-Non-polymers , 2 types, 95 molecules ![](data/chem/img/ATP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-ATP / |
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#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.31 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop / Details: Bird, L.E., (1998) Nucl. Acids Res., 26, 2686. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→10 Å / Num. obs: 42105 / % possible obs: 92.5 % / Observed criterion σ(I): 0 / Redundancy: 2.36 % / Rmerge(I) obs: 0.103 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / σ(F): 0 / Rfactor obs: 0.228 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |