+Open data
-Basic information
Entry | Database: PDB / ID: 1qhg | ||||||
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Title | STRUCTURE OF DNA HELICASE MUTANT WITH ADPNP | ||||||
Components | ATP-DEPENDENT HELICASE PCRA | ||||||
Keywords | HYDROLASE / DNA REPAIR / DNA REPLICATION / SOS RESPONSE / HELICASE / ATP-BINDING / DNA-BINDING | ||||||
Function / homology | Function and homology information 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 | Geobacillus stearothermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Soultanas, P. / Dillingham, M.S. / Velankar, S.S. / Wigley, D.B. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qhg.cif.gz | 146.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qhg.ent.gz | 113.3 KB | Display | PDB format |
PDBx/mmJSON format | 1qhg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qhg_validation.pdf.gz | 812.6 KB | Display | wwPDB validaton report |
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Full document | 1qhg_full_validation.pdf.gz | 845.1 KB | Display | |
Data in XML | 1qhg_validation.xml.gz | 28.8 KB | Display | |
Data in CIF | 1qhg_validation.cif.gz | 39.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qh/1qhg ftp://data.pdbj.org/pub/pdb/validation_reports/qh/1qhg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 82595.102 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Geobacillus stearothermophilus (bacteria) Strain: NCA1503 / Gene: PCRA / Plasmid: PET22 / Gene (production host): PCRA / Production host: Escherichia coli (E. coli) / References: UniProt: P56255 |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ATP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.7 Å3/Da / Density % sol: 66.77 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | ||||||||||||||||||||||||||||||||||||
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: SYNCHROTRON / Site: SRS / Type: SRS / Wavelength: 0.87 |
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: 37521 / % possible obs: 92.3 % / Observed criterion σ(I): 0 / Redundancy: 2.36 % / Rmerge(I) obs: 0.61 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→10 Å / Cross valid method: THROUGHOUT / σ(F): 0
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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: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.22 / Rfactor Rwork: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |