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- PDB-2isv: Structure of Giardia fructose-1,6-biphosphate aldolase in complex... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2isv | ||||||
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Title | Structure of Giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate | ||||||
![]() | Putative fructose-1,6-bisphosphate aldolase | ||||||
![]() | LYASE / Class II fructose-1 / 6-bisphosphate aldolase / glycolytic pathway / Giardia lamblia / drug target | ||||||
Function / homology | ![]() tagatose-bisphosphate aldolase activity / fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose 1,6-bisphosphate metabolic process / glycolytic process / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Galkin, A. / Herzberg, O. | ||||||
![]() | ![]() Title: Characterization, kinetics, and crystal structures of fructose-1,6-bisphosphate aldolase from the human parasite, Giardia lamblia. Authors: Galkin, A. / Kulakova, L. / Melamud, E. / Li, L. / Wu, C. / Mariano, P. / Dunaway-Mariano, D. / Nash, T.E. / Herzberg, O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.8 KB | Display | ![]() |
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PDB format | ![]() | 105.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458.5 KB | Display | ![]() |
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Full document | ![]() | 485.2 KB | Display | |
Data in XML | ![]() | 31.9 KB | Display | |
Data in CIF | ![]() | 44.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2iswC ![]() 1jvf C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Details | The biological assembly is a dimer generated from the molecules A and B in the asymmetric unit |
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Components
#1: Protein | Mass: 35293.785 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.62 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.75 Details: 18-23% Polyethylglycol monomethyl ether 2000, 0.1 M Tris-HCl, 0.2 M MgCl2, 20 mM PGH, pH 8.75, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 7, 2003 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. all: 31046 / Num. obs: 28450 / % possible obs: 91.6 % / Rmerge(I) obs: 0.037 |
Reflection shell | Resolution: 2.3→2.38 Å / Rmerge(I) obs: 0.116 / % possible all: 77.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1JVF ![]() 1jvf Resolution: 2.3→30 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 51.3 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.38 Å
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