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Yorodumi- PDB-5gxz: Crystal structure of endoglucanase CelQ from Clostridium thermoce... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5gxz | ||||||||||||
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Title | Crystal structure of endoglucanase CelQ from Clostridium thermocellum complexed with cellobiose and cellotriose | ||||||||||||
Components | Glucanase | ||||||||||||
Keywords | HYDROLASE / CELLULASES / GLYCOSYL HYDROLASE / CELLULOSOME | ||||||||||||
Function / homology | Function and homology information Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / cellulose binding / polysaccharide catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds Similarity search - Function | ||||||||||||
Biological species | Clostridium thermocellum (bacteria) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å | ||||||||||||
Authors | Jeng, W.Y. / Liu, C.I. / Wang, A.H.J. | ||||||||||||
Funding support | Taiwan, 3items
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Citation | Journal: Chembiochem / Year: 2019 Title: Crystal Structures of the C-Terminally Truncated Endoglucanase Cel9Q from Clostridium thermocellum Complexed with Cellodextrins and Tris. Authors: Jeng, W.Y. / Liu, C.I. / Lu, T.J. / Lin, H.J. / Wang, N.C. / Wang, A.H. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gxz.cif.gz | 532.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gxz.ent.gz | 431.6 KB | Display | PDB format |
PDBx/mmJSON format | 5gxz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gx/5gxz ftp://data.pdbj.org/pub/pdb/validation_reports/gx/5gxz | HTTPS FTP |
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-Related structure data
Related structure data | 5gxxC 5gxyC 5gy0C 5gy1C 1ga2S 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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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 69212.594 Da / Num. of mol.: 2 / Fragment: UNP residues 28-628 / Mutation: I251T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium thermocellum (bacteria) / Gene: celQ / Plasmid: pET-21a / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: Q9AJF8, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
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-Sugars , 2 types, 4 molecules
#2: Polysaccharide | #3: Polysaccharide | |
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-Non-polymers , 5 types, 1254 molecules
#4: Chemical | ChemComp-CA / #5: Chemical | ChemComp-CL / #6: Chemical | ChemComp-BR / #7: Chemical | ChemComp-7PE / | #8: 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: 2.96 Å3/Da / Density % sol: 58.46 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 9-12%(w/v) PEG3350, 15-20%(v/v) PEG550MME, 30mM NaBr, 30mM NaF and 30mM NaI, 0.1M Tris |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 0.97622 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 6, 2010 / Details: Vertically Focusing Mirror |
Radiation | Monochromator: Horizontally Focusing Single Crystal Si(111) Bent Monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97622 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→30 Å / Num. obs: 103578 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 4 % / Biso Wilson estimate: 29.7 Å2 / Rmerge(I) obs: 0.156 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 2.05→2.12 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.581 / Mean I/σ(I) obs: 2.9 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GA2 Resolution: 2.05→28.34 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.906 / SU B: 9.632 / SU ML: 0.118 / Cross valid method: THROUGHOUT / ESU R: 0.171 / ESU R Free: 0.163 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.409 Å2
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Refinement step | Cycle: 1 / Resolution: 2.05→28.34 Å
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Refine LS restraints |
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