+Open data
-Basic information
Entry | Database: PDB / ID: 1ryw | ||||||
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Title | C115S MurA liganded with reaction products | ||||||
Components | UDP-N-acetylglucosamine 1-carboxyvinyltransferase | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Eschenburg, S. / Schonbrunn, E. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Evidence That the Fosfomycin Target Cys115 in UDP-N-acetylglucosamine Enolpyruvyl Transferase (MurA) Is Essential for Product Release. Authors: Eschenburg, S. / Priestman, M. / Schonbrunn, E. | ||||||
History |
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Remark 600 | HETEROGEN HET GROUPS NUMBERED 2000+ ARE ASSOCIATED WITH CHAIN A. HET GROUPS NUMBERED 3000+ ARE ...HETEROGEN HET GROUPS NUMBERED 2000+ ARE ASSOCIATED WITH CHAIN A. HET GROUPS NUMBERED 3000+ ARE ASSOCIATED WITH CHAIN B. HET GROUPS NUMBERED 4000+ ARE ASSOCIATED WITH CHAIN C. HET GROUPS NUMBERED 5000+ ARE ASSOCIATED WITH CHAIN D. HET GROUPS NUMBERED 6000+ ARE ASSOCIATED WITH CHAIN E. HET GROUPS NUMBERED 7000+ ARE ASSOCIATED WITH CHAIN F. HET GROUPS NUMBERED 8000+ ARE ASSOCIATED WITH CHAIN G. HET GROUPS NUMBERED 9000+ ARE ASSOCIATED WITH CHAIN H. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ryw.cif.gz | 664.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ryw.ent.gz | 549.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ryw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ryw_validation.pdf.gz | 3.1 MB | Display | wwPDB validaton report |
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Full document | 1ryw_full_validation.pdf.gz | 3.1 MB | Display | |
Data in XML | 1ryw_validation.xml.gz | 142.7 KB | Display | |
Data in CIF | 1ryw_validation.cif.gz | 192.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ry/1ryw ftp://data.pdbj.org/pub/pdb/validation_reports/ry/1ryw | HTTPS FTP |
-Related structure data
Related structure data | 1ejcS S: Starting model for refinement |
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Similar 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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-Components
#1: Protein | Mass: 44813.344 Da / Num. of mol.: 8 / Mutation: N67D,C115S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacter cloacae (bacteria) / Gene: MURA, MURZ / Production host: Escherichia coli (E. coli) References: UniProt: P33038, UDP-N-acetylglucosamine 1-carboxyvinyltransferase #2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-EPU / #4: Chemical | ChemComp-GOL / #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: 2.27 Å3/Da / Density % sol: 45.84 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 20,000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 85 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 14, 2000 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. all: 140111 / Num. obs: 140111 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6 % / Rsym value: 0.1 / Net I/σ(I): 12 |
Reflection shell | Resolution: 2.3→2.34 Å / Redundancy: 4 % / Mean I/σ(I) obs: 3 / Num. unique all: 6835 / Rsym value: 0.35 / % possible all: 97.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ejc Resolution: 2.3→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.34 Å
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