+Open data
-Basic information
Entry | Database: PDB / ID: 3b8d | |||||||||
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Title | Fructose 1,6-bisphosphate aldolase from rabbit muscle | |||||||||
Components | Fructose-bisphosphate aldolase A | |||||||||
Keywords | LYASE / ALDOLASE / LYASE(ALDEHYDE) / SCHIFF BASE / GLYCOLYSIS / Acetylation / Phosphorylation | |||||||||
Function / homology | Function and homology information negative regulation of Arp2/3 complex-mediated actin nucleation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / fructose 1,6-bisphosphate metabolic process / I band / glycolytic process / protein homotetramerization / positive regulation of cell migration / cytosol Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Maurady, A. / Sygusch, J. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases. Authors: Maurady, A. / Zdanov, A. / De Moissac, D. / Beaudry, D. / Sygusch, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3b8d.cif.gz | 356 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3b8d.ent.gz | 281.2 KB | Display | PDB format |
PDBx/mmJSON format | 3b8d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b8/3b8d ftp://data.pdbj.org/pub/pdb/validation_reports/b8/3b8d | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 39262.688 Da / Num. of mol.: 4 / Mutation: E188Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: ALDOA / Plasmid: PPB1 / Production host: Escherichia coli (E. coli) / Strain (production host): DH5ALPHAMCR / References: UniProt: P00883, fructose-bisphosphate aldolase #2: Chemical | #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: 2.51 Å3/Da / Density % sol: 50.91 % |
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Crystal grow | Temperature: 293 K / Method: small tubes / pH: 7.4 Details: 40% ammonium sulphate 5mM EDTA, 100mM triethylamine, pH 7.4, SMALL TUBES, temperature 293K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 Å |
Detector | Type: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Jan 1, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→10 Å / Num. all: 88143 / Num. obs: 87623 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→10 Å / σ(F): 1 / σ(I): 1 / Stereochemistry target values: XPLOR parhcsdx
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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