+Open data
-Basic information
Entry | Database: PDB / ID: 1ex5 | ||||||
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Title | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE | ||||||
Components | FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE | ||||||
Keywords | LYASE / ALDOLASE / LYASE(ALDEHYDE) / SCHIFF BASE / GLYCOLYSIS | ||||||
Function / homology | Function and homology information negative regulation of Arp2/3 complex-mediated actin nucleation / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / M band / I band / glycolytic process / protein homotetramerization / positive regulation of cell migration Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 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 | 1ex5.cif.gz | 406.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ex5.ent.gz | 327.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ex5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ex/1ex5 ftp://data.pdbj.org/pub/pdb/validation_reports/ex/1ex5 | 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: 39205.637 Da / Num. of mol.: 4 / Mutation: E187A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Tissue: SKELETAL MUSCLE / Plasmid: PPB1 / Production host: Escherichia coli (E. coli) / Strain (production host): DH5ALPHAMCR / References: UniProt: P00883, fructose-bisphosphate aldolase #2: 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: 2.61 Å3/Da / Density % sol: 52.94 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: small tubes / pH: 7.4 Details: 40% ammonium sulphate, 5mM EDTA, pH 7.4, SMALL TUBES, temperature 293K | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: 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: 2.15→10 Å / Num. all: 88801 / Num. obs: 56675 / % possible obs: 98 % / Redundancy: 1.88 % |
Reflection shell | Resolution: 2.15→9 Å / Redundancy: 2.06 % / % possible all: 98 |
Reflection | *PLUS % possible obs: 81 % / Num. measured all: 88801 / Rmerge(I) obs: 0.077 |
-Processing
Software |
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Refinement | Resolution: 2.2→9 Å / σ(F): 1 / σ(I): 1 / Stereochemistry target values: XPLOR parhcsdx
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Refinement step | Cycle: LAST / Resolution: 2.2→9 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 9 Å / σ(F): 1 / % reflection Rfree: 8 % / Rfactor obs: 0.178 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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