+Open data
-Basic information
Entry | Database: PDB / ID: 1uae | ||||||
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Title | STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE | ||||||
Components | UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE | ||||||
Keywords | TRANSFERASE / PEPTIDOGLYCAN / UDP-N-ACETYLGLUCOSAMINE / FOSFOMYCIN | ||||||
Function / homology | Function and homology information UDP-N-acetylglucosamine 1-carboxyvinyltransferase / UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity / UDP-N-acetylgalactosamine biosynthetic process / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / cell cycle / cell division / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Skarzynski, T. | ||||||
Citation | Journal: Structure / Year: 1996 Title: Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Authors: Skarzynski, T. / Mistry, A. / Wonacott, A. / Hutchinson, S.E. / Kelly, V.A. / Duncan, K. #1: Journal: J.Bacteriol. / Year: 1992 Title: Cloning and Sequencing of Escherichia Coli Murz and Purification of its Product, a Udp-N-Acetylglucosamine Enolpyruvyl Transferase Authors: Marquardt, J.L. / Siegele, D.A. / Kolter, R. / Walsh, C.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uae.cif.gz | 101.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uae.ent.gz | 76.6 KB | Display | PDB format |
PDBx/mmJSON format | 1uae.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ua/1uae ftp://data.pdbj.org/pub/pdb/validation_reports/ua/1uae | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 44871.543 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) References: UniProt: P0A749, UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
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#2: Chemical | ChemComp-UD1 / |
#3: Chemical | ChemComp-FFQ / [( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 9, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Num. obs: 41471 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Rmerge(I) obs: 0.08 |
Reflection | *PLUS Highest resolution: 1.8 Å / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Resolution: 1.8→6 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 21.19 Å2 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | |||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.185 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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