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Yorodumi- PDB-5jqp: Crystal structure of ER glucosidase II heterodimeric complex cons... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5jqp | ||||||||||||||||||
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Title | Crystal structure of ER glucosidase II heterodimeric complex consisting of catalytic subunit and the binding domain of regulatory subunit | ||||||||||||||||||
Components |
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Keywords | HYDROLASE / PROTEIN TRANSPORT | ||||||||||||||||||
Function / homology | Function and homology information alpha-glucosidase / N-glycan processing / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / carbohydrate metabolic process / endoplasmic reticulum / metal ion binding Similarity search - Function | ||||||||||||||||||
Biological species | Chaetomium thermophilum (fungus) | ||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||||||||||||||
Authors | Satoh, T. / Toshimori, T. / Noda, M. / Uchiyama, S. / Kato, K. | ||||||||||||||||||
Funding support | Japan, 5items
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Citation | Journal: Protein Sci. / Year: 2016 Title: Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control. Authors: Satoh, T. / Toshimori, T. / Noda, M. / Uchiyama, S. / Kato, K. | ||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5jqp.cif.gz | 240.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5jqp.ent.gz | 185.1 KB | Display | PDB format |
PDBx/mmJSON format | 5jqp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jq/5jqp ftp://data.pdbj.org/pub/pdb/validation_reports/jq/5jqp | HTTPS FTP |
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-Related structure data
Related structure data | 5dkxS 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 108501.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: CTHT_0064960 / Plasmid: PCOLD-GST (MODIFIED) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: G0SG42 | ||
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#2: Protein | Mass: 17753.391 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 21-162 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: CTHT_0046400 / Plasmid: pET16b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: G0S9M2 | ||
#3: Chemical | ChemComp-TRS / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.1 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 20% PEG 3350, 100 mM Bis-Tris (pH 6.5), 0.2 M ammonium phosphate |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-1A / Wavelength: 1.1 Å |
Detector | Type: DECTRIS EIGER R 4M / Detector: PIXEL / Date: Dec 15, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 64671 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 4.4 % / Rmerge(I) obs: 0.108 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 2.2→2.24 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.499 / Mean I/σ(I) obs: 2.2 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5DKX Resolution: 2.2→20 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.935 / SU B: 5.189 / SU ML: 0.127 / Cross valid method: THROUGHOUT / ESU R: 0.206 / ESU R Free: 0.178 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.227 Å2
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Refinement step | Cycle: 1 / Resolution: 2.2→20 Å
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Refine LS restraints |
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