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Yorodumi- PDB-2a59: Structure of 6,7-Dimethyl-8-ribityllumazine synthase from Schizos... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2a59 | ||||||
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Title | Structure of 6,7-Dimethyl-8-ribityllumazine synthase from Schizosaccharomyces pombe mutant W27Y with bound ligand 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione | ||||||
Components | 6,7-dimethyl-8-ribityllumazine synthaseLumazine synthase | ||||||
Keywords | TRANSFERASE / 6 / 7-Dimethyl-8-ribityllumazine synthase / Schizosaccharomyces pombe / mutant W27Y / LUSY / 5-nitroso-6-ribitylamino-2 / 4(1H / 3H)-pyrimidinedione | ||||||
Function / homology | Function and homology information riboflavin synthase activity / riboflavin binding / 6,7-dimethyl-8-ribityllumazine synthase / 6,7-dimethyl-8-ribityllumazine synthase activity / riboflavin synthase complex / riboflavin biosynthetic process / mitochondrial intermembrane space / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.7 Å | ||||||
Authors | Koch, M. / Breithaupt, C. / Gerhardt, S. / Haase, I. / Weber, S. / Cushman, M. / Huber, R. / Bacher, A. / Fischer, M. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 2004 Title: Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase Authors: Koch, M. / Breithaupt, C. / Gerhardt, S. / Haase, I. / Weber, S. / Cushman, M. / Huber, R. / Bacher, A. / Fischer, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2a59.cif.gz | 147.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2a59.ent.gz | 118.7 KB | Display | PDB format |
PDBx/mmJSON format | 2a59.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a5/2a59 ftp://data.pdbj.org/pub/pdb/validation_reports/a5/2a59 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | the biological assembly is the pentamer found in the asymmetric unit |
-Components
#1: Protein | Mass: 17183.756 Da / Num. of mol.: 5 / Mutation: W27Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Gene: rib4 / Production host: Escherichia coli (E. coli) References: UniProt: Q9UUB1, 6,7-dimethyl-8-ribityllumazine synthase #2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-LMZ / #4: 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: 2.86 Å3/Da / Density % sol: 57 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5 Details: sodium citrate, ammonium dihydrogen phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 11, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. all: 28707 / Num. obs: 28707 / % possible obs: 99.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.9 % / Rmerge(I) obs: 0.109 / Rsym value: 0.109 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 2.7→2.78 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.482 / Mean I/σ(I) obs: 2.6 / Rsym value: 0.026 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 2.7→20 Å / Isotropic thermal model: isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 32.822 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.287 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Refine LS restraints |
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Xplor file |
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