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Yorodumi- PDB-6k78: Glycerol kinase form Thermococcus kodakarensis, complex structure... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6k78 | ||||||
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Title | Glycerol kinase form Thermococcus kodakarensis, complex structure with substrate. | ||||||
Components | (Glycerol kinase) x 2 | ||||||
Keywords | TRANSFERASE / Glycerol / Kinase / ATP / Archaea | ||||||
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 / cytosol Similarity search - Function | ||||||
Biological species | Thermococcus kodakarensis (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.301 Å | ||||||
Authors | Koga, Y. / Angkawidjaja, C. / Matsumura, H. / Hokao, R. | ||||||
Funding support | Japan, 1items
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Citation | Journal: To Be Published Title: Structural analysis of hexameric structure of glycerol kinase from Thermococcus kodakaraeinsis KOD1 Authors: Hokao, R. / Matsumura, H. / Katsumi, R. / Angkawidjaja, C. / Takano, K. / Kanaya, S. / Koga, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6k78.cif.gz | 377.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6k78.ent.gz | 307.9 KB | Display | PDB format |
PDBx/mmJSON format | 6k78.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k7/6k78 ftp://data.pdbj.org/pub/pdb/validation_reports/k7/6k78 | HTTPS FTP |
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-Related 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: 55984.422 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (archaea) Strain: ATCC BAA-918 / JCM 12380 / KOD1 / Gene: glpK, TK1396 / Production host: Escherichia coli (E. coli) / References: UniProt: O93623, glycerol kinase | ||||||||
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#2: Protein | Mass: 55969.410 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (archaea) Strain: ATCC BAA-918 / JCM 12380 / KOD1 / Gene: glpK, TK1396 / Production host: Escherichia coli (E. coli) / References: UniProt: O93623, glycerol kinase #3: Chemical | ChemComp-PGE / #4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.05 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: imidazole, PEG1000, Calcium acetate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å |
Detector | Type: AGILENT ATLAS CCD / Detector: CCD / Date: Jul 15, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 89647 / % possible obs: 98.6 % / Redundancy: 4 % / Net I/σ(I): 23.6 |
Reflection shell | Resolution: 2.3→2.34 Å / Num. unique obs: 4385 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.301→32.194 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.97 / Phase error: 30.3
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.301→32.194 Å
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Refine LS restraints |
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LS refinement shell |
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