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- PDB-3gay: 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: 3gay | ||||||
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Title | Structure of Giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate | ||||||
![]() | Fructose-bisphosphate aldolase | ||||||
![]() | LYASE / Class II fructose-1 / 6-bisphosphate aldolase / glycolytic pathway / Giardia lamblia / drug target / Glycolysis | ||||||
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: Structural insights into the substrate binding and stereoselectivity of giardia fructose-1,6-bisphosphate aldolase. Authors: Galkin, A. / Li, Z. / Li, L. / Kulakova, L. / Pal, L.R. / Dunaway-Mariano, D. / 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 | ![]() | 146.3 KB | Display | ![]() |
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PDB format | ![]() | 113.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 31.3 KB | Display | |
Data in CIF | ![]() | 46.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3gakC ![]() 3gb6C ![]() 2iswS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 35263.758 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | AUTHORS STATE THAT ACCORDING TO THE SEQUENCE FROM GIARDIA GENOME (GB ENTRY EAA46366.1) THE CORRECT ...AUTHORS STATE THAT ACCORDING TO THE SEQUENCE FROM GIARDIA GENOME (GB ENTRY EAA46366.1) THE CORRECT RESIDUE AT POSITION 129 IS GLY. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.86 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 18-25% PEG3350, 0.2M NH4NO3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Apr 9, 2007 / Details: mirrors |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. all: 61609 / Num. obs: 57851 / % possible obs: 93.9 % / Rmerge(I) obs: 0.066 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.342 / % possible all: 62.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2ISW Resolution: 1.8→20 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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