|Entry||Database: PDB / ID: 1zal|
|Title||Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially disordered tagatose-1,6-bisphosphate, a weak competitive inhibitor|
|Components||Fructose-bisphosphate aldolase A|
|Keywords||LYASE / aldolase / weak competitive inhibitor / non covalent complex / tagatose-1 / 6-bisphosphate|
|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
Fructose-bisphosphate aldolase class-I active site. / Fructose-bisphosphate aldolase class-I active site / Fructose-bisphosphate aldolase class-I / Fructose-bisphosphate aldolase, class-I / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Fructose-bisphosphate aldolase A
Similarity search - Component
|Biological species||Oryctolagus cuniculus (rabbit)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.89 Å|
|Authors||St-Jean, M. / Lafrance-Vanasse, J. / Liotard, B. / Sygusch, J.|
|Citation||Journal: J.Biol.Chem. / Year: 2005|
Title: High Resolution Reaction Intermediates of Rabbit Muscle Fructose-1,6-bisphosphate Aldolase: substrate cleavage and induced fit.
Authors: St-Jean, M. / Lafrance-Vanasse, J. / Liotard, B. / Sygusch, J.
|Remark 600||HETEROGEN Electron density associated with tagatose-1,6-bisphosphate was not clearly defined and ...HETEROGEN Electron density associated with tagatose-1,6-bisphosphate was not clearly defined and only phosphate groups that were visible in the active sites of the enzyme were refined as PO4 ions.|
|Structure viewer||Molecule: |
Downloads & links
A: Fructose-bisphosphate aldolase A
B: Fructose-bisphosphate aldolase A
C: Fructose-bisphosphate aldolase A
D: Fructose-bisphosphate aldolase A
|Details||The biological assembly is the homotetramer found in the asymmetric unit|
Mass: 39263.672 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: ALDOA / Plasmid: pPB14 / Production host: Escherichia coli (E. coli) / Strain (production host): BL-21 SI (Invitrogen) / References: UniProt: P00883, fructose-bisphosphate aldolase
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.28 Å3/Da / Density % sol: 46.1 %|
|Crystal grow||Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: NSLS / Beamline: X8C / Wavelength: 1 Å|
|Detector||Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 1, 2004|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1 Å / Relative weight: 1|
|Reflection||Resolution: 1.68→50 Å / Num. all: 161207 / Num. obs: 134418 / % possible obs: 83.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.07 / Χ2: 0.922|
|Reflection shell||Resolution: 1.68→1.74 Å / % possible obs: 30.3 % / Redundancy: 1.7 % / Rmerge(I) obs: 0.766 / Num. measured obs: 4874 / Χ2: 0.651 / % possible all: 30.3|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: PDB ENTRY 1ADO
Resolution: 1.89→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 1 / Stereochemistry target values: Engh & Huber
Details: The PO4 ions were refined to half occupancy as well as the water molecules located at the same loci. Both were declared as alternate conformations during refinement.
|Solvent computation||Bsol: 73.225 Å2|
|Displacement parameters||Biso mean: 30.86 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.89→50 Å|
|Refine LS restraints|
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