+Open data
-Basic information
Entry | Database: PDB / ID: 5syh | |||||||||
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Title | Structure of D141A variant of B. pseudomallei KatG | |||||||||
Components | Catalase-peroxidase | |||||||||
Keywords | OXIDOREDUCTASE / catalase-peroxidase / KatG / D141A variant | |||||||||
Function / homology | Function and homology information catalase-peroxidase / catalase activity / hydrogen peroxide catabolic process / response to oxidative stress / heme binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Burkholderia pseudomallei (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | |||||||||
Authors | Loewen, P.C. | |||||||||
Funding support | Canada, 1items
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Citation | Journal: J. Am. Chem. Soc. / Year: 2014 Title: An ionizable active-site tryptophan imparts catalase activity to a peroxidase core. Authors: Loewen, P.C. / Carpena, X. / Vidossich, P. / Fita, I. / Rovira, C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5syh.cif.gz | 576.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5syh.ent.gz | 464.8 KB | Display | PDB format |
PDBx/mmJSON format | 5syh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sy/5syh ftp://data.pdbj.org/pub/pdb/validation_reports/sy/5syh | HTTPS FTP |
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-Related structure data
Related structure data | 5sykC 1mwv C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 0
NCS ensembles :
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 79524.977 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Burkholderia pseudomallei (strain 1710b) (bacteria) Strain: 1710b / Gene: katG, BURPS1710b_3366 / Production host: Escherichia coli (E. coli) / References: UniProt: Q3JNW6, catalase-peroxidase |
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-Non-polymers , 7 types, 1596 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-MPD / ( #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.14 Å3/Da / Density % sol: 60.81 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion Details: 16-20% PEG 4000, 20% MPD, 0.1 M sodium citrate pH 5.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.98 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 21, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→95.14 Å / Num. obs: 228125 / % possible obs: 95.2 % / Redundancy: 3.9 % / Rsym value: 0.087 / Net I/σ(I): 8.8 |
Reflection shell | Resolution: 1.65→1.74 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.403 / Mean I/σ(I) obs: 1.8 / Num. measured all: 121936 / Num. unique all: 31995 / % possible all: 92.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1MWV 1mwv Resolution: 1.65→20 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.964 / SU B: 2.699 / SU ML: 0.046 / SU R Cruickshank DPI: 0.0666 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.067 / ESU R Free: 0.071 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 106.29 Å2 / Biso mean: 21.871 Å2 / Biso min: 9.62 Å2
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Refinement step | Cycle: final / Resolution: 1.65→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05
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LS refinement shell | Resolution: 1.65→1.693 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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