+Open data
-Basic information
Entry | Database: PDB / ID: 1f0k | ||||||
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Title | THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG | ||||||
Components | UDP-N-ACETYLGLUCOSAMINE-N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE | ||||||
Keywords | TRANSFERASE / Rossmann fold | ||||||
Function / homology | Function and homology information undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase / undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity / UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity / lipid glycosylation / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / carbohydrate metabolic process / cell cycle / cell division / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å | ||||||
Authors | Ha, S. / Walker, D. / Shi, Y. / Walker, S. | ||||||
Citation | Journal: Protein Sci. / Year: 2000 Title: The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Authors: Ha, S. / Walker, D. / Shi, Y. / Walker, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f0k.cif.gz | 144.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f0k.ent.gz | 113.5 KB | Display | PDB format |
PDBx/mmJSON format | 1f0k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1f0k_validation.pdf.gz | 436.8 KB | Display | wwPDB validaton report |
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Full document | 1f0k_full_validation.pdf.gz | 451.4 KB | Display | |
Data in XML | 1f0k_validation.xml.gz | 29.6 KB | Display | |
Data in CIF | 1f0k_validation.cif.gz | 42.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f0/1f0k ftp://data.pdbj.org/pub/pdb/validation_reports/f0/1f0k | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 39060.992 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET21B / Production host: Escherichia coli (E. coli) References: UniProt: P17443, Transferases; Glycosyltransferases; Hexosyltransferases #2: Chemical | ChemComp-SO4 / | #3: 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: 2.85 Å3/Da / Density % sol: 56.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: NaMES, ammonium sulfate, TritonX-100, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.9 Details: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 1.0092 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 11, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0092 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. all: 65567 / Num. obs: 65567 / % possible obs: 97.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4.4 % / Biso Wilson estimate: 26 Å2 / Rmerge(I) obs: 0.032 / Net I/σ(I): 41.9 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 3.79 % / Rmerge(I) obs: 0.187 / Num. unique all: 6450 / % possible all: 96.4 |
Reflection | *PLUS Num. measured all: 288150 |
Reflection shell | *PLUS % possible obs: 96.4 % / Mean I/σ(I) obs: 7 |
-Processing
Software |
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Refinement | Resolution: 1.9→40 Å / σ(F): 2 / σ(I): 2
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Refinement step | Cycle: LAST / Resolution: 1.9→40 Å
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Refine LS restraints |
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Software | *PLUS Name: 'CNS' / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.247 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |