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- PDB-1eyn: Structure of mura liganded with the extrinsic fluorescence probe ANS -
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Open data
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Basic information
Entry | Database: PDB / ID: 1eyn | ||||||
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Title | Structure of mura liganded with the extrinsic fluorescence probe ANS | ||||||
![]() | UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE | ||||||
![]() | TRANSFERASE / inside-out alpha-beta barrel / L-isoaspartate in position 67 | ||||||
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 / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schonbrunn, E. / Eschenburg, S. / Luger, K. / Kabsch, W. / Amrhein, N. | ||||||
![]() | ![]() Title: Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Authors: Schonbrunn, E. / Eschenburg, S. / Luger, K. / Kabsch, W. / Amrhein, N. #1: ![]() Title: Comparative X-ray Analysis of the Un-liganded Fosfomycin-Target MurA Authors: Eschenburg, S. / Schonbrunn, E. #2: ![]() Title: Role of the Loop Containing Residue 115 in the Induced-fit Mechanism of the Bacterial Cell Wall Biosynthetic Enzyme MurA Authors: Schonbrunn, E. / Eschenburg, S. / Krekel, F. / Luger, K. / Amrhein, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 107.6 KB | Display | ![]() |
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PDB format | ![]() | 80.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.2 KB | Display | ![]() |
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Full document | ![]() | 475.9 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 19.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ejcS 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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Unit cell |
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Components
#1: Protein | Mass: 44829.406 Da / Num. of mol.: 1 / Mutation: N67D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P33038, UDP-N-acetylglucosamine 1-carboxyvinyltransferase | ||
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#2: Chemical | ChemComp-2AN / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.51 % | ||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: MES/PEG20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Nov 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.542 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→29.33 Å / Num. all: 1222364 / Num. obs: 49890 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 24 % / Biso Wilson estimate: 21.1 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 20 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 10 % / Rmerge(I) obs: 0.29 / % possible all: 98.3 |
Reflection | *PLUS Num. measured all: 1222364 |
Reflection shell | *PLUS % possible obs: 98.3 % / Mean I/σ(I) obs: 2.6 |
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Processing
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Refinement | Starting model: 1EJC Resolution: 1.7→29.33 Å / Isotropic thermal model: Restrained / σ(F): 0 / σ(I): 0 / Stereochemistry target values: engh & huber
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Solvent computation | Solvent model: Flat Model / Bsol: 85.013 Å2 / ksol: 0.4529 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.7→29.33 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.81 Å / Rfactor Rfree error: 0.025 / Total num. of bins used: 6
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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