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Yorodumi- PDB-1fwy: CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSF... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fwy | ||||||
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Title | CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC | ||||||
Components | UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE | ||||||
Keywords | TRANSFERASE / acetyltransferase / bifunctional / drug design / pyrophosphorylase | ||||||
Function / homology | Function and homology information glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape ...glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape / magnesium ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Brown, K. / Pompeo, F. / Dixon, S. / Mengin-Lecreulx, D. / Cambillau, C. / Bourne, Y. | ||||||
Citation | Journal: EMBO J. / Year: 1999 Title: Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. Authors: Brown, K. / Pompeo, F. / Dixon, S. / Mengin-Lecreulx, D. / Cambillau, C. / Bourne, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fwy.cif.gz | 137.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fwy.ent.gz | 114.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fwy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fw/1fwy ftp://data.pdbj.org/pub/pdb/validation_reports/fw/1fwy | HTTPS FTP |
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-Related structure data
-Links
-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 biological assembly is a trimer either from chain A or B |
-Components
#1: Protein | Mass: 36174.090 Da / Num. of mol.: 2 / Fragment: TRUNCATED FORM AFTER R331 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET-22B / Production host: Escherichia coli (E. coli) References: UniProt: P0ACC7, UDP-N-acetylglucosamine diphosphorylase #2: Chemical | ChemComp-SO4 / #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.84 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 1.3-1.5 M ammonium sulfate, 0.1 M MES, 4% acetone (v/v), pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.93 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 12, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 40 / % possible obs: 97.3 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 5.1 |
Reflection shell | *PLUS % possible obs: 98.1 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 1.6 |
-Processing
Software |
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Refinement | Resolution: 2.3→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 40231 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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