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- PDB-5ggi: Crystal structure of human protein O-mannose beta-1,2-N-acetylglu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ggi | |||||||||
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Title | Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Mn, UDP and Mannosyl-peptide | |||||||||
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![]() | TRANSFERASE / SUGAR BINDING PROTEIN/SUBSTRATE / glycosyltransferease / O-mannosylation / alpha-dystroglycan / SUGAR BINDING PROTEIN-SUBSTRATE complex | |||||||||
Function / homology | ![]() beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity / Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3 / O-linked glycosylation / localization of cell / protein O-linked mannosylation / reactive gliosis / O-glycan processing / acetylglucosaminyltransferase activity / basement membrane organization / dentate gyrus development ...beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity / Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3 / O-linked glycosylation / localization of cell / protein O-linked mannosylation / reactive gliosis / O-glycan processing / acetylglucosaminyltransferase activity / basement membrane organization / dentate gyrus development / protein O-linked glycosylation / Transferases; Glycosyltransferases; Hexosyltransferases / myelination / sensory perception of sound / manganese ion binding / gene expression / carbohydrate binding / Golgi membrane / membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Kuwabara, N. / Senda, T. / Kato, R. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan Authors: Kuwabara, N. / Manya, H. / Yamada, T. / Tateno, H. / Kanagawa, M. / Kobayashi, K. / Akasaka-Manya, K. / Hirose, Y. / Mizuno, M. / Ikeguchi, M. / Toda, T. / Hirabayashi, J. / Senda, T. / Endo, T. / Kato, R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 408.3 KB | Display | ![]() |
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PDB format | ![]() | 333.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 36.3 KB | Display | |
Data in CIF | ![]() | 49.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ggfC ![]() 5gggSC ![]() 5ggjC ![]() 5ggkC ![]() 5gglC ![]() 5ggnC ![]() 5ggoC ![]() 5ggpC C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein / Protein/peptide / Sugars , 3 types, 6 molecules ABFG![](data/chem/img/MAN.gif)
![](data/chem/img/MAN.gif)
#1: Protein | Mass: 65551.453 Da / Num. of mol.: 2 / Fragment: UNP residues 92-660 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q8WZA1, Transferases; Glycosyltransferases; Hexosyltransferases #2: Protein/peptide | Mass: 817.951 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #6: Sugar | |
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-Non-polymers , 4 types, 106 molecules ![](data/chem/img/UDP.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-PO4 / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.2 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: NaKPO4 / PH range: 6.6-6.8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Jul 21, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→46.37 Å / Num. obs: 46907 / % possible obs: 100 % / Redundancy: 26.2 % / Rmerge(I) obs: 0.338 / Net I/σ(I): 20.5 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 11.8 % / Rmerge(I) obs: 1.085 / Mean I/σ(I) obs: 2.1 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5GGG Resolution: 2.6→46.372 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 25.31 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→46.372 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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