+Open data
-Basic information
Entry | Database: PDB / ID: 1ejc | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of unliganded mura (type2) | ||||||
Components | UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYLTRANSFERASE | ||||||
Keywords | TRANSFERASE / inside-out alpha/beta barrel | ||||||
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 / cytoplasm Similarity search - Function | ||||||
Biological species | Enterobacter cloacae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Eschenburg, S. / Schonbrunn, E. | ||||||
Citation | Journal: Proteins / Year: 2000 Title: Comparative X-ray analysis of the un-liganded fosfomycin-target murA. Authors: Eschenburg, S. / Schonbrunn, E. #1: Journal: Biochemistry / Year: 2000 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. #2: Journal: Structure / Year: 1996 Title: Crystal Structure of UDP-N-acetylglucosamine Enolpyruvyltransferase, the Target of the Antibiotic Fosfomycin Authors: Schonbrunn, E. / Sack, S. / Eschenburg, S. / Perrakis, A. / Krekel, F. / Amrhein, N. / Mandelkow, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1ejc.cif.gz | 102.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1ejc.ent.gz | 81.7 KB | Display | PDB format |
PDBx/mmJSON format | 1ejc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ejc_validation.pdf.gz | 446.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1ejc_full_validation.pdf.gz | 452.2 KB | Display | |
Data in XML | 1ejc_validation.xml.gz | 23.1 KB | Display | |
Data in CIF | 1ejc_validation.cif.gz | 36.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ej/1ejc ftp://data.pdbj.org/pub/pdb/validation_reports/ej/1ejc | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 44829.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacter cloacae (bacteria) / Production host: Escherichia coli (E. coli) References: UniProt: P33038, UDP-N-acetylglucosamine 1-carboxyvinyltransferase | ||
---|---|---|---|
#2: Chemical | ChemComp-PO4 / | ||
#3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.89 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10 % PEG 20000, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 120 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 5, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. all: 36451 / Num. obs: 36451 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.8 % / Biso Wilson estimate: 17.3 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 28.4 |
Reflection shell | Resolution: 1.8→1.84 Å / Rmerge(I) obs: 0.225 / % possible all: 99.2 |
Reflection | *PLUS Num. measured all: 251049 |
Reflection shell | *PLUS % possible obs: 99.2 % / Mean I/σ(I) obs: 5.8 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.8→20 Å / Rfactor Rfree error: 0.006 / Isotropic thermal model: restrained / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: HOH 1 occupies an alternate position of alternate conformation A NH1 ARG 295. HOH 1 has alternate position A.
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 19 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: NONE | |||||||||||||||||||||||||
LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.022 / Total num. of bins used: 6
| |||||||||||||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|