+Open data
-Basic information
Entry | Database: PDB / ID: 3h3o | ||||||
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Title | Glycerol Kinase H232R with Ethylene Glycol | ||||||
Components | Glycerol kinase | ||||||
Keywords | TRANSFERASE / ethylene glycol / kinase / ATP-binding / Glycerol metabolism / Nucleotide-binding / Phosphoprotein | ||||||
Function / homology | Function and homology information glycerol kinase / glycerol kinase activity / glycerol-3-phosphate metabolic process / glycerol metabolic process / glycerol catabolic process / phosphorylation / ATP binding Similarity search - Function | ||||||
Biological species | Enterococcus casseliflavus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / PHASER / Resolution: 2.3 Å | ||||||
Authors | Yeh, J.I. / Kettering, R.D. | ||||||
Citation | Journal: Biochemistry / Year: 2009 Title: Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation Authors: Yeh, J.I. / Kettering, R. / Saxl, R. / Bourand, A. / Darbon, E. / Joly, N. / Briozzo, P. / Deutscher, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3h3o.cif.gz | 386.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3h3o.ent.gz | 316.5 KB | Display | PDB format |
PDBx/mmJSON format | 3h3o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h3/3h3o ftp://data.pdbj.org/pub/pdb/validation_reports/h3/3h3o | HTTPS FTP |
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-Related structure data
Related structure data | 3d7eC 3flcC 3h3nC 3h45C 3h46C 1xupS 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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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 55831.535 Da / Num. of mol.: 4 / Mutation: H232R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterococcus casseliflavus (bacteria) / Gene: glpK / Plasmid: pOXO4 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109(DE3) / References: UniProt: O34153, glycerol kinase #2: Chemical | ChemComp-EDO / #3: Chemical | ChemComp-PO4 / #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: 2.41 Å3/Da / Density % sol: 49 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion Details: KH2PO4, PEG 8000, VAPOR DIFFUSION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.97 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 20, 2008 / Details: Si(111) |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→49.5 Å / Num. obs: 92379 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rsym value: 0.082 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 2.1 / Rsym value: 0.528 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: PHASER Starting model: PDB ENTRY 1XUP Resolution: 2.3→10 Å / Occupancy max: 1 / Occupancy min: 1 / σ(F): 3 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
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Displacement parameters | Biso max: 113.62 Å2 / Biso mean: 51.997 Å2 / Biso min: 17.48 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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