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Yorodumi- PDB-5ggl: Crystal structure of N-terminal domain of human protein O-mannose... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ggl | |||||||||
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Title | Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-alpha-pNP | |||||||||
Components | Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 | |||||||||
Keywords | SUGAR BINDING PROTEIN / glycosyltransferease / O-mannosylation / alpha-dystroglycan | |||||||||
Function / homology | Function and homology information 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 / reactive gliosis / protein O-linked mannosylation / 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 / reactive gliosis / protein O-linked mannosylation / O-glycan processing / acetylglucosaminyltransferase activity / basement membrane organization / dentate gyrus development / protein O-linked glycosylation / Transferases; Glycosyltransferases; Hexosyltransferases / myelination / sensory perception of sound / gene expression / manganese ion binding / carbohydrate binding / Golgi membrane / membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.27 Å | |||||||||
Authors | Kuwabara, N. / Senda, T. / Kato, R. | |||||||||
Funding support | Japan, 2items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2016 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ggl.cif.gz | 145 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ggl.ent.gz | 112.6 KB | Display | PDB format |
PDBx/mmJSON format | 5ggl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gg/5ggl ftp://data.pdbj.org/pub/pdb/validation_reports/gg/5ggl | HTTPS FTP |
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-Related structure data
Related structure data | 5ggfC 5gggSC 5ggiC 5ggjC 5ggkC 5ggnC 5ggoC 5ggpC C: citing same article (ref.) S: Starting model for refinement |
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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 on special symmetry positions |
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-Components
#1: Protein | Mass: 17623.020 Da / Num. of mol.: 2 / Fragment: UNP residues 92-250 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POMGNT1, MGAT1.2, UNQ746/PRO1475 / Production host: Escherichia coli (E. coli) References: UniProt: Q8WZA1, Transferases; Glycosyltransferases; Hexosyltransferases #2: Sugar | #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: 2.29 Å3/Da / Density % sol: 46.29 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.8 / Details: Tris-HCl, PEG-8000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 10, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.27→42.1 Å / Num. obs: 86073 / % possible obs: 100 % / Redundancy: 12.7 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 1.27→1.29 Å / Redundancy: 12.4 % / Rmerge(I) obs: 1.84 / Mean I/σ(I) obs: 1.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5GGG Resolution: 1.27→42.124 Å / SU ML: 0.11 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 15.87 / 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: 1.27→42.124 Å
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Refine LS restraints |
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LS refinement shell |
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