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Yorodumi- PDB-6h91: Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6h91 | |||||||||
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Title | Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.4 A | |||||||||
Components | Beta-phosphoglucomutase | |||||||||
Keywords | ISOMERASE / phosphoglucomutase / phospho-enzyme / acetylphosphate | |||||||||
Function / homology | Function and homology information beta-phosphoglucomutase / beta-phosphoglucomutase activity / carbohydrate metabolic process / magnesium ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Lactococcus lactis subsp. lactis Il1403 (lactic acid bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å | |||||||||
Authors | Robertson, A.J. / Bisson, C. / Waltho, J.P. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: To Be Published Title: Transition state of phospho-enzyme hydrolysis in beta-phosphoglucomutase Authors: Robertson, A.J. / Bisson, C. / Waltho, J.P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6h91.cif.gz | 100.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6h91.ent.gz | 75.8 KB | Display | PDB format |
PDBx/mmJSON format | 6h91.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h9/6h91 ftp://data.pdbj.org/pub/pdb/validation_reports/h9/6h91 | HTTPS FTP |
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-Related structure data
Related structure data | 6h92C 2wheS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24319.574 Da / Num. of mol.: 2 / Mutation: K125R, Y206H Source method: isolated from a genetically manipulated source Details: Residue D8 is modified by phosphorylation in the pre-formed crystal. Source: (gene. exp.) Lactococcus lactis subsp. lactis Il1403 (lactic acid bacteria) Gene: pgmB, LL0429, L0001 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P71447, beta-phosphoglucomutase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-EDO / | #5: 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: 2.42 Å3/Da / Density % sol: 49.23 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: 24-34% PEG 4000, 200 mM sodium acetate, 50 mM TRIS pH 7.5, The crystal was cryoprotected in its original mother liquor plus an additional 25% ethylene glycol and 30mM acetylphosphate. PH range: 7.2 / Temp details: 100 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97779 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 23, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97779 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→58.62 Å / Num. obs: 18430 / % possible obs: 99 % / Redundancy: 3.7 % / CC1/2: 0.987 / Rmerge(I) obs: 0.12 / Rpim(I) all: 0.084 / Rrim(I) all: 0.165 / Net I/σ(I): 6.7 |
Reflection shell | Resolution: 2.38→2.44 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.597 / Num. unique obs: 1355 / CC1/2: 0.526 / Rpim(I) all: 0.438 / Rrim(I) all: 0.813 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2WHE Resolution: 2.38→58.62 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.875 / SU B: 13.495 / SU ML: 0.303 / Cross valid method: THROUGHOUT / ESU R: 0.537 / ESU R Free: 0.325 / 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: 40.3 Å2
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Refinement step | Cycle: 1 / Resolution: 2.38→58.62 Å
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Refine LS restraints |
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