+Open data
-Basic information
Entry | Database: PDB / ID: 4rz5 | ||||||
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Title | Transaldolase B E96Q from E.coli | ||||||
Components | Transaldolase BTransaldolase | ||||||
Keywords | TRANSFERASE / TalB / Tim barrel / homodimer / Transaldolase of Pentose phosphate pathway | ||||||
Function / homology | Function and homology information transketolase or transaldolase activity / transaldolase / transaldolase activity / pentose-phosphate shunt, non-oxidative branch / carbohydrate metabolic process / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Stellmacher, L. / Sandalova, T. / Leptihn, S. / Schneider, G. / Sprenger, G.A. / Samland, A.K. | ||||||
Citation | Journal: ChemCatChem / Year: 2015 Title: Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase Authors: Stellmacher, L. / Sandalova, T. / Leptihn, S. / Schneider, G. / Sprenger, G.A. / Samland, A.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rz5.cif.gz | 274.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rz5.ent.gz | 222.6 KB | Display | PDB format |
PDBx/mmJSON format | 4rz5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rz/4rz5 ftp://data.pdbj.org/pub/pdb/validation_reports/rz/4rz5 | HTTPS FTP |
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-Related structure data
Related structure data | 4rxfC 4rxgC 4rz4C 4rz6C 4s1fC 1onrS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: THR / Beg label comp-ID: THR / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 0 / Auth seq-ID: 2 - 317 / Label seq-ID: 22 - 337
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-Components
#1: Protein | Mass: 37459.559 Da / Num. of mol.: 2 / Mutation: E96Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b0008, JW0007, talB, yaaK / Plasmid: pJF119 / Production host: Escherichia coli (E. coli) Strain (production host): LJ110(DE3) talA- talB- pLysS RARE2 References: UniProt: P0A870, transaldolase #2: Chemical | ChemComp-SO4 / #3: 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: 2.65 Å3/Da / Density % sol: 53.61 % |
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Crystal grow | Temperature: 293.2 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.15M Li2SO4, 23% PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.2K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9763 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 14, 2013 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→46.92 Å / Num. all: 74166 / Num. obs: 74166 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Biso Wilson estimate: 18.4 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 1.8 / Num. unique all: 4351 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1ONR, monomer Resolution: 1.8→46.92 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.917 / SU B: 8 / SU ML: 0.11 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.189 / ESU R Free: 0.133 / 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: 26.993 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→46.92 Å
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Refine LS restraints |
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