+Open data
-Basic information
Entry | Database: PDB / ID: 3ec2 | ||||||
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Title | Crystal structure of the DnaC helicase loader | ||||||
Components | DNA replication protein DnaC | ||||||
Keywords | REPLICATION / helicase loader / replication initiation factor / ATP-binding / Nucleotide-binding | ||||||
Function / homology | Function and homology information DNA replication / ATP hydrolysis activity / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | Aquifex aeolicus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.7 Å | ||||||
Authors | Mott, M.L. / Erzberger, J.P. / Coons, M.M. / Berger, J.M. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2008 Title: Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators. Authors: Mott, M.L. / Erzberger, J.P. / Coons, M.M. / Berger, J.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ec2.cif.gz | 46.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ec2.ent.gz | 35.9 KB | Display | PDB format |
PDBx/mmJSON format | 3ec2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3ec2_validation.pdf.gz | 800.3 KB | Display | wwPDB validaton report |
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Full document | 3ec2_full_validation.pdf.gz | 817.7 KB | Display | |
Data in XML | 3ec2_validation.xml.gz | 12.5 KB | Display | |
Data in CIF | 3ec2_validation.cif.gz | 16.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ec/3ec2 ftp://data.pdbj.org/pub/pdb/validation_reports/ec/3ec2 | 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: 20812.529 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Gene: dnaC, aq_910 / Production host: Escherichia coli (E. coli) / References: UniProt: O67056 |
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#2: Chemical | ChemComp-ADP / |
#3: Chemical | ChemComp-MG / |
#4: Water | ChemComp-HOH / |
-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: 51.39 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 50mM Tris, 1% PEG 6K, 1mM TCEP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 0.9795, 1.11587 | |||||||||
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 16, 2005 | |||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2.25→50 Å / Num. obs: 5534 / Biso Wilson estimate: 39.424 Å2 / Rsym value: 0.05 |
-Processing
Software |
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Refinement | Resolution: 2.7→50 Å / WRfactor Rfree: 0.282 / WRfactor Rwork: 0.221 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.761 / SU Rfree: 0.408 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso max: 111.26 Å2 / Biso mean: 67.597 Å2 / Biso min: 21.88 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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