+Open data
-Basic information
Entry | Database: PDB / ID: 2dwo | ||||||
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Title | PFKFB3 in complex with ADP and PEP | ||||||
Components | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 | ||||||
Keywords | TRANSFERASE / HYDROLASE / Bifunctional enzyme | ||||||
Function / homology | Function and homology information 6-phosphofructo-2-kinase / 6-phosphofructo-2-kinase activity / fructose 2,6-bisphosphate metabolic process / fructose-2,6-bisphosphate 2-phosphatase / fructose-2,6-bisphosphate 2-phosphatase activity / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / fructose metabolic process / nucleoplasm / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Lee, Y.H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: A Direct Substrate-Substrate Interaction Found in the Kinase Domain of the Bifunctional Enzyme, 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase Authors: Kim, S.G. / Cavalier, M. / El-Maghrabi, M.R. / Lee, Y.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2dwo.cif.gz | 114.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dwo.ent.gz | 85.7 KB | Display | PDB format |
PDBx/mmJSON format | 2dwo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dw/2dwo ftp://data.pdbj.org/pub/pdb/validation_reports/dw/2dwo | HTTPS FTP |
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-Related structure data
Related structure data | 2dwpC 2i1vC 2axnS 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 59694.137 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PFKFB3 / Production host: Escherichia coli (E. coli) References: UniProt: Q16875, 6-phosphofructo-2-kinase, fructose-2,6-bisphosphate 2-phosphatase |
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#2: Sugar | ChemComp-F6P / |
#3: Chemical | ChemComp-ADP / |
#4: Chemical | ChemComp-PEP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.38 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: PEG 4000, ETHYLENE GLYCOL, TRIS-PHOSHATE, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CAMD / Beamline: GCPCC / Wavelength: 1.3808 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: May 12, 2006 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.3808 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→30 Å / Num. obs: 38937 / % possible obs: 99.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.25→2.33 Å / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2AXN Resolution: 2.25→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.25→30 Å
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Refine LS restraints |
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