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Open data
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Basic information
| Entry | Database: PDB / ID: 6xi2 | ||||||
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| Title | Apo form of POMGNT2 | ||||||
Components |
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Keywords | TRANSFERASE / muscular dystrophy / alpha-dystroglycan / O-mannosylation / POMGNT2 | ||||||
| Function / homology | Function and homology informationprotein O-mannose beta-1,4-N-acetylglucosaminyltransferase / O-linked glycosylation / protein O-linked glycosylation via mannose / protein O-acetylglucosaminyltransferase activity / acetylglucosaminyltransferase activity / protein O-linked glycosylation / neuron migration / endoplasmic reticulum membrane / endoplasmic reticulum Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.57 Å | ||||||
Authors | Halmo, S.M. / Yeh, J. / Wells, L. / Moremen, K.W. / Lanzilotta, W.N. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2021Title: Crystal structures of beta-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies. Authors: Yang, J.Y. / Halmo, S.M. / Praissman, J. / Chapla, D. / Singh, D. / Wells, L. / Moremen, K.W. / Lanzilotta, W.N. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6xi2.cif.gz | 438.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6xi2.ent.gz | 348.9 KB | Display | PDB format |
| PDBx/mmJSON format | 6xi2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6xi2_validation.pdf.gz | 522.6 KB | Display | wwPDB validaton report |
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| Full document | 6xi2_full_validation.pdf.gz | 549.3 KB | Display | |
| Data in XML | 6xi2_validation.xml.gz | 71.3 KB | Display | |
| Data in CIF | 6xi2_validation.cif.gz | 97.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xi/6xi2 ftp://data.pdbj.org/pub/pdb/validation_reports/xi/6xi2 | HTTPS FTP |
-Related 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 O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase ... , 4 types, 4 molecules ABDC
| #1: Protein | Mass: 61017.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POMGNT2, AGO61, C3orf39, EOGTL, GTDC2 / Production host: Homo sapiens (human)References: UniProt: Q8NAT1, protein O-mannose beta-1,4-N-acetylglucosaminyltransferase |
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| #2: Protein | Mass: 60240.426 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POMGNT2, AGO61, C3orf39, EOGTL, GTDC2 / Production host: Homo sapiens (human)References: UniProt: Q8NAT1, protein O-mannose beta-1,4-N-acetylglucosaminyltransferase |
| #3: Protein | Mass: 60972.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POMGNT2, AGO61, C3orf39, EOGTL, GTDC2 / Production host: Homo sapiens (human)References: UniProt: Q8NAT1, protein O-mannose beta-1,4-N-acetylglucosaminyltransferase |
| #4: Protein | Mass: 60143.316 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POMGNT2, AGO61, C3orf39, EOGTL, GTDC2 / Production host: Homo sapiens (human)References: UniProt: Q8NAT1, protein O-mannose beta-1,4-N-acetylglucosaminyltransferase |
-Protein/peptide , 2 types, 2 molecules GH
| #5: Protein/peptide | Mass: 728.793 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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| #6: Protein/peptide | Mass: 700.741 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-Sugars , 1 types, 3 molecules 
| #7: Sugar |
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-Non-polymers , 2 types, 173 molecules 


| #8: Chemical | ChemComp-PO4 / #9: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 4.29 Å3/Da / Density % sol: 71.32 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.1 M potassium/sodium tartrate, 0.1 M Bis-Tris, pH 7.9, 10% PEG8000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
| Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Feb 13, 2016 |
| Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 2.57→50 Å / Num. obs: 131723 / % possible obs: 99.1 % / Redundancy: 14.6 % / CC1/2: 0.864 / CC star: 0.963 / Net I/σ(I): 21.3 |
| Reflection shell | Resolution: 2.57→2.66 Å / Num. unique obs: 12111 / CC1/2: 0.864 / CC star: 0.963 |
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Processing
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| Refinement | Method to determine structure: SAD / Resolution: 2.57→45.99 Å / SU ML: 0.3 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 25.19 / 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: 144.08 Å2 / Biso mean: 48.964 Å2 / Biso min: 21.21 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: final / Resolution: 2.57→45.99 Å
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14
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About Yorodumi




Homo sapiens (human)
X-RAY DIFFRACTION
United States, 1items
Citation








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