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Open data
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Basic information
Entry | Database: PDB / ID: 1uae | ||||||
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Title | STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE | ||||||
![]() | UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE | ||||||
![]() | TRANSFERASE / PEPTIDOGLYCAN / UDP-N-ACETYLGLUCOSAMINE / FOSFOMYCIN | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Skarzynski, T. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.3 KB | Display | ![]() |
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PDB format | ![]() | 76.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.7 KB | Display | ![]() |
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Full document | ![]() | 478.1 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 18.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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.) ![]() ![]() 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: ![]() |
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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: ![]() ![]() ![]() |
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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 |
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Processing
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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: ![]() | |||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.185 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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