+Open data
-Basic information
Entry | Database: PDB / ID: 2cn2 | ||||||
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Title | Crystal Structures of Clostridium thermocellum Xyloglucanase | ||||||
Components | BETA-1,4-XYLOGLUCAN HYDROLASE | ||||||
Keywords | HYDROLASE / GH74 FAMILY / XYLOGLUCANASE / GLYCOSYLHYDROLASE | ||||||
Function / homology | Function and homology information xyloglucan-specific endo-beta-1,4-glucanase activity / xyloglucan catabolic process / cellulosome / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / cellulose catabolic process Similarity search - Function | ||||||
Biological species | CLOSTRIDIUM THERMOCELLUM (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Martinez-Fleites, C. / Taylor, E.J. / Guerreiro, C.I. / Prates, J.A.M. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Baumann, M.J. / Brumer, H. / Davies, G.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Crystal Structures of Clostridium Thermocellum Xyloglucanase, Xgh74A, Reveal the Structural Basis for Xyloglucan Recognition and Degradation. Authors: Martinez-Fleites, C. / Guerreiro, C.I. / Baumann, M.J. / Taylor, E.J. / Prates, J.A.M. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Brumer, H. / Davies, G.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2cn2.cif.gz | 579.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2cn2.ent.gz | 477.9 KB | Display | PDB format |
PDBx/mmJSON format | 2cn2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/2cn2 ftp://data.pdbj.org/pub/pdb/validation_reports/cn/2cn2 | HTTPS FTP |
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-Related structure data
Related structure data | 2cn3C 1sqjS 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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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 81849.695 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CLOSTRIDIUM THERMOCELLUM (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): TUNER References: UniProt: Q70DK5, xyloglucan-specific endo-beta-1,4-glucanase #2: Chemical | ChemComp-CD / #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: 3.03 Å3/Da / Density % sol: 59 % |
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Crystal grow | Details: 5MM CDCL2, 12% PEG 4K, NA CACODYLATE PH 6.5 |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 20, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→45.79 Å / Num. obs: 220410 / % possible obs: 99 % / Observed criterion σ(I): 2 / Redundancy: 3.9 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.5 / % possible all: 98.3 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1SQJ Resolution: 2.1→19.9 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.926 / SU B: 3.848 / SU ML: 0.103 / Cross valid method: THROUGHOUT / ESU R: 0.174 / ESU R Free: 0.153 / 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: 19.36 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→19.9 Å
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Refine LS restraints |
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