+Open data
-Basic information
Entry | Database: PDB / ID: 2cn3 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal Structures of Clostridium thermocellum Xyloglucanase | |||||||||
Components | BETA-1,4-XYLOGLUCAN HYDROLASE | |||||||||
Keywords | HYDROLASE / GLYCOSYLHYDROLASE / FAMILY GH74 / XYLOGLUCANASE | |||||||||
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: 1.95 Å | |||||||||
Authors | Martinez-Fleites, C. / Taylor, E.J. / Guerreiro, C.I.P.D. / 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. / Taylor, E.J. / Guerreiro, C.I.P.D. / Prates, J.A.M. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Baumann, M.J. / Brumer, H. / Davies, G.J. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2cn3.cif.gz | 322.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2cn3.ent.gz | 259.3 KB | Display | PDB format |
PDBx/mmJSON format | 2cn3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/2cn3 ftp://data.pdbj.org/pub/pdb/validation_reports/cn/2cn3 | HTTPS FTP |
---|
-Related structure data
Related structure data | 2cn2SC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 80961.586 Da / Num. of mol.: 2 / Fragment: RESIDUES 28-764 / Mutation: YES 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: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D- ...alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59 % |
---|---|
Crystal grow | Details: 20% PEG3350, HEPES PH 7.5, 0.2M KSCN |
-Data collection
Diffraction | Mean temperature: 120 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97565 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 1, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97565 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→57.07 Å / Num. obs: 142508 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 11.5 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 1.95→2.06 Å / Redundancy: 11.5 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 4.6 / % possible all: 100 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2CN2 Resolution: 1.95→19.96 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.95 / SU B: 2.814 / SU ML: 0.082 / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.125 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 15.64 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→19.96 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|