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Yorodumi- PDB-2fjk: Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fjk | ||||||
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Title | Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus | ||||||
Components | Fructose-bisphosphate aldolase | ||||||
Keywords | LYASE / beta-alpha-barrels | ||||||
Function / homology | Function and homology information fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose 1,6-bisphosphate metabolic process / glycolytic process / zinc ion binding Similarity search - Function | ||||||
Biological species | Thermus caldophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.2 Å | ||||||
Authors | Lee, J.H. / Im, Y.J. / Rho, S.-H. / Kim, M.-K. / Kang, G.B. / Eom, S.H. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2006 Title: Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus Authors: Lee, J.H. / Bae, J. / Kim, D. / Choi, Y. / Im, Y.J. / Koh, S. / Kim, J.S. / Kim, M.-K. / Kang, G.B. / Hong, S.-I. / Lee, D.-S. / Eom, S.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fjk.cif.gz | 229 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fjk.ent.gz | 195.1 KB | Display | PDB format |
PDBx/mmJSON format | 2fjk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2fjk_validation.pdf.gz | 470.1 KB | Display | wwPDB validaton report |
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Full document | 2fjk_full_validation.pdf.gz | 524 KB | Display | |
Data in XML | 2fjk_validation.xml.gz | 52 KB | Display | |
Data in CIF | 2fjk_validation.cif.gz | 69.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fj/2fjk ftp://data.pdbj.org/pub/pdb/validation_reports/fj/2fjk | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a tetramer. The asymmetric unit contains biological tetramer molecules (Chain A,B,C and D). |
-Components
#1: Protein | Mass: 33411.070 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus caldophilus (bacteria) / Plasmid: pKK223-3 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q703I2, fructose-bisphosphate aldolase #2: Chemical | ChemComp-13P / #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: 2.42 Å3/Da / Density % sol: 49.17 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 18% PEG 10000, 0.1M potassium cloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 110 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-18B / Wavelength: 0.9797, 0.9795, 0.9600 | ||||||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 23, 2000 | ||||||||||||
Radiation | Monochromator: GRAPHITE / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.2→50 Å / Num. obs: 68172 / % possible obs: 98 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 | ||||||||||||
Reflection shell | Resolution: 2.2→2.3 Å / % possible all: 95.2 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.2→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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