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Yorodumi- PDB-1g97: S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+ -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g97 | ||||||
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Title | S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+ | ||||||
Components | N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE | ||||||
Keywords | TRANSFERASE / GlmU / acetyltransferase / uridyltransferase / pyrophosphorylase / left-handed beta-sheet helix / trimer / magnesium / UDP-N-acetylglucosamine | ||||||
Function / homology | Function and homology information glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell wall organization / cell morphogenesis / regulation of cell shape ...glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell wall organization / cell morphogenesis / regulation of cell shape / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Streptococcus pneumoniae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.96 Å | ||||||
Authors | Kostrewa, D. / D'Arcy, A. / Kamber, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution. Authors: Kostrewa, D. / D'Arcy, A. / Takacs, B. / Kamber, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g97.cif.gz | 112.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g97.ent.gz | 83.9 KB | Display | PDB format |
PDBx/mmJSON format | 1g97.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g9/1g97 ftp://data.pdbj.org/pub/pdb/validation_reports/g9/1g97 | HTTPS FTP |
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-Related structure data
Related structure data | 1g95SC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is a trimer generated from the monomer in the asymmetric unit by the operations: -Y+1, X-Y, Z and -X+Y+1, -X+1, Z |
-Components
#1: Protein | Mass: 49398.387 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Production host: Escherichia coli (E. coli) References: UniProt: Q97R46, UDP-N-acetylglucosamine diphosphorylase |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-NA / |
#4: Chemical | ChemComp-UD1 / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.9 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M BIS/TRIS, 0.2 M Ammonium Sulfate, 25 % PEG 3350, soaked with 10 mM UDP-N-Acetylglucosamine and 10 mM Mg(Cl)2, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||
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: ESRF / Beamline: BM1A / Wavelength: 0.873 / Wavelength: 0.873 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 25, 1998 / Details: Mirrors |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→30 Å / Num. all: 81753 / Num. obs: 33249 / % possible obs: 98 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Biso Wilson estimate: 19.1 Å2 / Rsym value: 0.062 / Net I/σ(I): 14.9 |
Reflection shell | Resolution: 1.96→2.03 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 3.6 / Num. unique all: 3197 / Rsym value: 0.311 / % possible all: 95.4 |
Reflection | *PLUS Rmerge(I) obs: 0.062 |
Reflection shell | *PLUS % possible obs: 95.4 % / Rmerge(I) obs: 0.311 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: Apo form of GlmU, PDB entry code 1G95 Resolution: 1.96→30 Å / Isotropic thermal model: isotropic / Cross valid method: FREE-R / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: BULK SOLVENT CORRECTION WITH ELECTRON DENSITY = 0.34 E/A**3, B-FACTOR = 26.9 A**2. WATER MOLECULES ARE ORDERED WITH ASCENDING B-FACTORS. THE FOLLOWING AMINO ACID RESIDUES WERE NOT VISIBLE IN ...Details: BULK SOLVENT CORRECTION WITH ELECTRON DENSITY = 0.34 E/A**3, B-FACTOR = 26.9 A**2. WATER MOLECULES ARE ORDERED WITH ASCENDING B-FACTORS. THE FOLLOWING AMINO ACID RESIDUES WERE NOT VISIBLE IN THE ELECTRON DENSITY MAPS: 1 and 448-459. THE FOLLOWING AMINO ACIDS HAVE HIGH AVERAGE B-FACTORS (>= 50 A**2) AND POOR ELECTRON DENSITY: 61, 90-92, 120-122, 145-146, 179, 188-190, 387-391, 441, 447.
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Solvent computation | Solvent model: bulk solvent mask / Bsol: 26.9 Å2 / ksol: 0.34 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.96→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.96→2.03 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / σ(F): 0 / % reflection Rfree: 4.9 % / Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 27.2 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.286 / % reflection Rfree: 4.6 % / Rfactor Rwork: 0.256 |