+Open data
-Basic information
Entry | Database: PDB / ID: 2wlu | ||||||
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Title | Iron-bound crystal structure of Streptococcus pyogenes Dpr | ||||||
Components | DPS-LIKE PEROXIDE RESISTANCE PROTEIN | ||||||
Keywords | OXIDOREDUCTASE / DNA-BINDING | ||||||
Function / homology | Function and homology information oxidoreductase activity, acting on metal ions / ferroxidase / ferroxidase activity / ferric iron binding / DNA binding Similarity search - Function | ||||||
Biological species | STREPTOCOCCUS PYOGENES (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 1.94 Å | ||||||
Authors | Haikarainen, T. / Tsou, C.-C. / Wu, J.-J. / Papageorgiou, A.C. | ||||||
Citation | Journal: J.Biol.Inorg.Chem. / Year: 2010 Title: Crystal Structures of Streptococcus Pyogenes Dpr Reveal a Dodecameric Iron-Binding Protein with a Ferroxidase Site. Authors: Haikarainen, T. / Tsou, C.-C. / Wu, J.-J. / Papageorgiou, A.C. #1: Journal: Infect.Immun. / Year: 2008 Title: An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus Pyogenes Against Multiple Stresses. Authors: Tsou, C. / Chiang-Ni, C. / Lin, Y. / Chuang, W. / Lin, M. / Liu, C. / Wu, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wlu.cif.gz | 52.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wlu.ent.gz | 39.6 KB | Display | PDB format |
PDBx/mmJSON format | 2wlu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2wlu_validation.pdf.gz | 436.8 KB | Display | wwPDB validaton report |
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Full document | 2wlu_full_validation.pdf.gz | 437.2 KB | Display | |
Data in XML | 2wlu_validation.xml.gz | 11.1 KB | Display | |
Data in CIF | 2wlu_validation.cif.gz | 16 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wl/2wlu ftp://data.pdbj.org/pub/pdb/validation_reports/wl/2wlu | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 19336.750 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) STREPTOCOCCUS PYOGENES (bacteria) / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: Q5XAZ8, UniProt: Q99YU7*PLUS, ferroxidase | ||
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#2: Chemical | ChemComp-NA / | ||
#3: Chemical | ChemComp-FE / | ||
#4: Chemical | #5: 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: 3.2 Å3/Da / Density % sol: 61 % / Description: NONE |
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Crystal grow | pH: 7 Details: 0.1M HEPES PH 7.0, 1M SUCCINIC ACID PH 7.0, 1% W/V PEG 2000 MME, 5% 2-PROPANOL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X13 / Wavelength: 0.8132 |
Detector | Type: MARRESEARCH SX-165 / Detector: CCD / Date: Feb 13, 2009 / Details: BENT, VERTICALLY FOCUSSING |
Radiation | Monochromator: SI (111), HORIZONTALLY FOCUSSING / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8132 Å / Relative weight: 1 |
Reflection | Resolution: 1.93→43 Å / Num. obs: 20355 / % possible obs: 92.7 % / Observed criterion σ(I): 2 / Redundancy: 7.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 16 |
Reflection shell | Resolution: 1.93→2.03 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 4.9 / % possible all: 79.1 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 1.94→43 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.957 / SU B: 1.754 / SU ML: 0.052 / Cross valid method: THROUGHOUT / ESU R: 0.102 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.381 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.94→43 Å
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Refine LS restraints |
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