[English] 日本語
Yorodumi- PDB-1xff: Glutaminase domain of glucosamine 6-phosphate synthase complexed ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xff | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate | |||||||||
Components | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] | |||||||||
Keywords | TRANSFERASE / COMPLEX (TRANSFERASE-INHIBITOR) / GLUTAMINE AMIDOTRANSFERASE | |||||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | |||||||||
Authors | Isupov, M.N. / Teplyakov, A. | |||||||||
Citation | Journal: Structure / Year: 1996 Title: Substrate Binding is Required for Assembly of the Active Conformation of the Catalytic Site in Ntn Amidotransferases: Evidence from the 1.8 Angstrom Crystal Structure of the Glutaminase Domain ...Title: Substrate Binding is Required for Assembly of the Active Conformation of the Catalytic Site in Ntn Amidotransferases: Evidence from the 1.8 Angstrom Crystal Structure of the Glutaminase Domain of Glucosamine 6-Phosphate Synthase Authors: Isupov, M.N. / Obmolova, G. / Butterworth, S. / Badet-Denisot, M.-A. / Badet, B. / Polikarpov, I. / Littlechild, J.A. / Teplyakov, A. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystallization and Preliminary X-Ray Analysis of the Two Domains of Glucosamine-6-Phosphate Synthase from Escherichia Coli Authors: Obmolova, G. / Badet-Denisot, M.A. / Badet, B. / Teplyakov, A. #2: Journal: J.Mol.Biol. / Year: 2001 Title: Channeling of Ammonia in Glucosamine 6-Phosphate Synthase Authors: Teplyakov, A. / Obmolova, G. / Badet-Denisot, M.A. / Badet, B. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1xff.cif.gz | 113.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1xff.ent.gz | 86.8 KB | Display | PDB format |
PDBx/mmJSON format | 1xff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xff_validation.pdf.gz | 456.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1xff_full_validation.pdf.gz | 463.7 KB | Display | |
Data in XML | 1xff_validation.xml.gz | 23 KB | Display | |
Data in CIF | 1xff_validation.cif.gz | 32.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xf/1xff ftp://data.pdbj.org/pub/pdb/validation_reports/xf/1xff | HTTPS FTP |
-Related structure data
Related structure data | 1xfgC 1gphS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 26507.059 Da / Num. of mol.: 2 / Fragment: GLUTAMINASE DOMAIN Source method: isolated from a genetically manipulated source Details: inhibited by L-GLUTAMATE / Source: (gene. exp.) Escherichia coli (E. coli) / Strain: 3000HFR / Gene: GLMS / Plasmid: PGM10A / Production host: Escherichia coli (E. coli) References: UniProt: P17169, glutamine-fructose-6-phosphate transaminase (isomerizing) #2: Chemical | #3: Chemical | ChemComp-ACT / | #4: Chemical | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.6 % |
---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M cacodylate, 1 M sodium acetate, 20% PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 295 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.99 / Wavelength: 0.99 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 8, 1993 / Details: MIRROR |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→24 Å / Num. obs: 47043 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 5.2 % / Biso Wilson estimate: 18.3 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 1.8→1.82 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.283 / Mean I/σ(I) obs: 3 / % possible all: 97.1 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GPH Resolution: 1.8→20 Å / Cor.coef. Fo:Fc: 0.973 / SU B: 1.645 / SU ML: 0.052 / Cross valid method: none used / σ(F): 0 / ESU R: 0.105 / Stereochemistry target values: MAXIMUM LIKELIHOOD
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.5 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.105 Å / Luzzati sigma a obs: 0.052 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.8→1.846 Å / Total num. of bins used: 20
|