+Open data
-Basic information
Entry | Database: PDB / ID: 1naw | ||||||
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Title | ENOLPYRUVYL TRANSFERASE | ||||||
Components | UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYL-TRANSFERASE | ||||||
Keywords | TRANSFERASE / PEPTIDOGLYCAN BIOSYNTHESIS / HINGE / DOMAIN MOVEMENT / SEQUENCE MOTIF / FOLDING | ||||||
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 division / cytoplasm Similarity search - Function | ||||||
Biological species | Enterobacter cloacae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2 Å | ||||||
Authors | Schoenbrunn, E. / Sack, S. / Eschenburg, S. / Perrakis, A. / Krekel, F. / Amrhein, N. / Mandelkow, E. | ||||||
Citation | 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. #1: Journal: J.Struct.Biol. / Year: 1996 Title: Crystallization and Preliminary X-Ray Diffraction Analysis of Udp-N-Acetylglucosamine Enolpyruvyltransferase of Enterobacter Cloacae Authors: Sack, S. / Dauter, Z. / Wanke, C. / Amrhein, N. / Mandelkow, E. / Schonbrunn, E. #2: Journal: FEBS Lett. / Year: 1992 Title: The Udp-N-Acetylglucosamine 1-Carboxyvinyl-Transferase of Enterobacter Cloacae. Molecular Cloning, Sequencing of the Gene and Overexpression of the Enzyme Authors: Wanke, C. / Falchetto, R. / Amrhein, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1naw.cif.gz | 179.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1naw.ent.gz | 139.9 KB | Display | PDB format |
PDBx/mmJSON format | 1naw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/1naw ftp://data.pdbj.org/pub/pdb/validation_reports/na/1naw | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 44828.422 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacter cloacae (bacteria) / Plasmid: PKK233-2 / Production host: Escherichia coli (E. coli) / Strain (production host): JM 105 (PHARMACIA LKB) References: UniProt: P33038, UDP-N-acetylglucosamine 1-carboxyvinyltransferase #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | ENOLPYRUVY | |
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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: 3.3 Å3/Da / Density % sol: 63 % | ||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.4 Details: CRYSTALS WERE GROWN BY THE HANGING DROP VAPOR DIFFUSION METHOD USING PLASTIC TISSUE CULTURE PLATES. 0.4 M SODIUM/POTASSIUM PHOSPHATE BUFFER (PH 6.4) CONTAINING 40 MM CYCLOHEXYLAMMONIUM ...Details: CRYSTALS WERE GROWN BY THE HANGING DROP VAPOR DIFFUSION METHOD USING PLASTIC TISSUE CULTURE PLATES. 0.4 M SODIUM/POTASSIUM PHOSPHATE BUFFER (PH 6.4) CONTAINING 40 MM CYCLOHEXYLAMMONIUM PHOSPHATE WERE EQUILIBRATED AGAINST 1 ML 0.8 M SODIUM/POTASSIUM PHOSPHATE BUFFER (PH 6.4). CRYSTALLIZATION USUALLY OCCURRED WITHIN 3 DAYS AND THE CRYSTALS REACHED THEIR MAXIMUM SIZE OF 0.5 X 0.5 X 0.1 MM==3== AFTER 5 DAYS AT ROOM TEMPERATURE. (SEE REFERENCE 1 FOR DETAILS.), vapor diffusion - hanging drop Temp details: room temp | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.99 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 27, 1995 |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→25 Å / Num. obs: 103189 / % possible obs: 99.8 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.053 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.29 / % possible all: 98.7 |
Reflection | *PLUS Num. measured all: 744941 |
Reflection shell | *PLUS % possible obs: 98.7 % |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2→10 Å
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Displacement parameters | Biso mean: 23.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 10 Å / Luzzati sigma a obs: 0.24 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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