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Yorodumi- PDB-3zy5: Crystal structure of POFUT1 in complex with GDP-fucose (crystal-f... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3zy5 | ||||||
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Title | Crystal structure of POFUT1 in complex with GDP-fucose (crystal-form-I) | ||||||
Components | PUTATIVE GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1 | ||||||
Keywords | TRANSFERASE / GLYCOSYLTRANSFERASE / GT-B / CATALYTIC MECHANISM / GT65 | ||||||
Function / homology | Function and homology information peptide-O-fucosyltransferase / protein O-linked fucosylation / peptide-O-fucosyltransferase activity / fucosyltransferase activity / fucose metabolic process / protein O-linked glycosylation / Notch signaling pathway / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | CAENORHABDITIS ELEGANS (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.96 Å | ||||||
Authors | Lira-Navarrete, E. / Valero-Gonzalez, J. / Villanueva, R. / Martinez-Julvez, M. / Tejero, T. / Merino, P. / Panjikar, S. / Hurtado-Guerrero, R. | ||||||
Citation | Journal: Plos One / Year: 2011 Title: Structural Insights Into the Mechanism of Protein O-Fucosylation. Authors: Lira-Navarrete, E. / Valero-Gonzalez, J. / Villanueva, R. / Martinez-Julvez, M. / Tejero, T. / Merino, P. / Panjikar, S. / Hurtado-Guerrero, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zy5.cif.gz | 164.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zy5.ent.gz | 128.1 KB | Display | PDB format |
PDBx/mmJSON format | 3zy5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zy/3zy5 ftp://data.pdbj.org/pub/pdb/validation_reports/zy/3zy5 | HTTPS FTP |
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-Related structure data
Related structure data | 3zy2SC 3zy3C 3zy4C 3zy6C 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
#1: Protein | Mass: 41008.746 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-383 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CAENORHABDITIS ELEGANS (invertebrata) / Production host: PICHIA PASTORIS (fungus) / Strain (production host): X-33 / References: UniProt: Q18014, peptide-O-fucosyltransferase | ||||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-GFB / | #4: Chemical | ChemComp-BTB / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ROTATING ANODE / Site: ESRF / Beamline: BM16 / Type: BRUKER / Wavelength: 1.54 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→56.01 Å / Num. obs: 42027 / % possible obs: 98 % / Observed criterion σ(I): 2 / Redundancy: 7.06 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 12.19 |
Reflection shell | Resolution: 1.96→2.06 Å / Redundancy: 5.01 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 12.19 / % possible all: 94.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3ZY2 Resolution: 1.96→93.08 Å / Cor.coef. Fo:Fc: 0.913 / Cor.coef. Fo:Fc free: 0.873 / SU B: 9.103 / SU ML: 0.123 / Cross valid method: THROUGHOUT / ESU R: 0.173 / ESU R Free: 0.166 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.265 Å2
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Refinement step | Cycle: LAST / Resolution: 1.96→93.08 Å
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Refine LS restraints |
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