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Open data
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Basic information
Entry | Database: PDB / ID: 1jxa | ||||||
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Title | GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE | ||||||
![]() | glucosamine 6-phosphate synthase | ||||||
![]() | TRANSFERASE / beta-sandwich / nucleotide-binding fold / gene duplication / ammonia channel | ||||||
Function / homology | ![]() glutamine-fructose-6-phosphate transaminase (isomerizing) / glutamine-fructose-6-phosphate transaminase (isomerizing) activity / UDP-N-acetylglucosamine metabolic process / UDP-N-acetylglucosamine biosynthetic process / carbohydrate derivative binding / fructose 6-phosphate metabolic process / protein N-linked glycosylation / glutamine metabolic process / carbohydrate metabolic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Teplyakov, A. / Obmolova, G. / Badet, B. / Badet-Denisot, M.A. | ||||||
![]() | ![]() Title: Channeling of ammonia in glucosamine-6-phosphate synthase. Authors: Teplyakov, A. / Obmolova, G. / Badet, B. / Badet-Denisot, M.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 355.4 KB | Display | ![]() |
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PDB format | ![]() | 287.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1gdo ![]() 1moqS 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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2 | ![]()
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Unit cell |
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Details | The second part of one biological homodimer is generated by the two-fold axis (-x, y, -z) applied to chain A. Another dimer is formed by chains B and C. |
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Components
#1: Protein | Mass: 66818.000 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P17169, glutamine-fructose-6-phosphate transaminase (isomerizing) #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.39 Å3/Da / Density % sol: 63.69 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: LiCl, PEG4K, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Details: Obmolova, G., (1994) J.Mol.Biol., 242, 703. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 8, 1998 / Details: CYLINDRICAL MIRROR |
Radiation | Monochromator: Ge(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→20 Å / Num. all: 45685 / Num. obs: 45685 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Biso Wilson estimate: 74.5 Å2 / Rmerge(I) obs: 0.056 |
Reflection shell | Resolution: 3.1→3.2 Å / Mean I/σ(I) obs: 2.8 / % possible all: 92 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 111045 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1MOQ, 1GDO Resolution: 3.1→12 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.1→12 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 12 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor all: 0.22 / Rfactor obs: 0.2 / Rfactor Rfree: 0.28 / Rfactor Rwork: 0.2 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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