+Open data
-Basic information
Entry | Database: PDB / ID: 5e9u | |||||||||
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Title | Crystal structure of GtfA/B complex bound to UDP and GlcNAc | |||||||||
Components |
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Keywords | TRANSFERASE/CHAPERONE / Glycosyltransferase / Accessory protein translocation / Complex / TRANSFERASE-CHAPERONE complex | |||||||||
Function / homology | Function and homology information protein O-linked glycosylation via serine / protein N-acetylglucosaminyltransferase complex / protein O-linked glycosylation / Transferases; Glycosyltransferases; Hexosyltransferases / glycosyltransferase activity / regulation of protein stability / nucleotide binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Streptococcus gordonii (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.84 Å | |||||||||
Authors | Chen, Y. / Rapoport, T.A. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2016 Title: Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Authors: Chen, Y. / Seepersaud, R. / Bensing, B.A. / Sullam, P.M. / Rapoport, T.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5e9u.cif.gz | 769.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5e9u.ent.gz | 626.1 KB | Display | PDB format |
PDBx/mmJSON format | 5e9u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5e9u_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 5e9u_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 5e9u_validation.xml.gz | 136.9 KB | Display | |
Data in CIF | 5e9u_validation.cif.gz | 182.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e9/5e9u ftp://data.pdbj.org/pub/pdb/validation_reports/e9/5e9u | HTTPS FTP |
-Related structure data
Related structure data | 5e9tSC 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 58399.207 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus gordonii (bacteria) / Strain: M99 / Gene: gtf1, gtfA / Production host: Escherichia coli (E. coli) References: UniProt: Q9AET5, Transferases; Glycosyltransferases; Hexosyltransferases #2: Protein | Mass: 51578.770 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus gordonii (bacteria) / Strain: M99 / Gene: gtf2, gtfB / Production host: Escherichia coli (E. coli) / References: UniProt: Q79T00 #3: Chemical | #4: Sugar | #5: Chemical | ChemComp-MG / Has protein modification | Y | |
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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: 3.58 Å3/Da / Density % sol: 65.63 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 4000, magnesium chloride, Tris, glycyl-glycyl-glycine PH range: 7.5 - 8.0 |
-Data collection
Diffraction | Mean temperature: 80 K | |||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.9792 Å | |||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 9, 2014 | |||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 | |||||||||||||||||||||||||||
Reflection | Resolution: 3.84→148.98 Å / Num. obs: 60983 / % possible obs: 100 % / Redundancy: 7.3 % / Biso Wilson estimate: 111.56 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.385 / Rpim(I) all: 0.166 / Net I/σ(I): 5.28 / Num. measured all: 448209 | |||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5E9T Resolution: 3.84→94.481 Å / SU ML: 0.63 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 38.6 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 309.3 Å2 / Biso mean: 115.4901 Å2 / Biso min: 31.83 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.84→94.481 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 27
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