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Yorodumi- PDB-4avn: Thermobifida fusca cellobiohydrolase Cel6B catalytic mutant D226A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4avn | |||||||||
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Title | Thermobifida fusca cellobiohydrolase Cel6B catalytic mutant D226A- S232A cocrystallized with cellobiose | |||||||||
Components | CELLOBIOHYDROLASE. GLYCOSYL HYDROLASE FAMILY 6 | |||||||||
Keywords | HYDROLASE / CELLULOSE DEGRADATION / GLYCOSIDE HYDROLASE FAMILY 6 / CELLULASE | |||||||||
Function / homology | Function and homology information Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / polysaccharide binding / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / metal ion binding Similarity search - Function | |||||||||
Biological species | THERMOBIFIDA FUSCA (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Wu, M. / Vuong, T.V. / Wilson, D.B. / Sandgren, M. / Stahlberg, J. / Hansson, H. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Loop Motions Important to Product Expulsion in the Thermobifida Fusca Glycoside Hydrolase Family 6 Cellobiohydrolase from Structural and Computational Studies. Authors: Wu, M. / Bu, L. / Vuong, T.V. / Wilson, D.B. / Crowley, M.F. / Sandgren, M. / Stahlberg, J. / Beckham, G.T. / Hansson, H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4avn.cif.gz | 101.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4avn.ent.gz | 75.3 KB | Display | PDB format |
PDBx/mmJSON format | 4avn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/av/4avn ftp://data.pdbj.org/pub/pdb/validation_reports/av/4avn | HTTPS FTP |
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-Related 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: 45413.738 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 177-596 / Mutation: YES Source method: isolated from a genetically manipulated source Details: CATALYTIC DOMAIN IS RESIDUES 139-558 IN MATURE PROTEIN Source: (gene. exp.) THERMOBIFIDA FUSCA (bacteria) / Strain: YX / Plasmid: PET / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): RPIL References: UniProt: Q47SA9, cellulose 1,4-beta-cellobiosidase (non-reducing end) |
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#2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellotetraose |
#3: Sugar | ChemComp-BGC / |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.84 % / Description: NONE |
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Crystal grow | pH: 4 Details: 20% PEG 6000, 0.1 M CALCIUM CHLORIDE, 0.1 M SODIUM ACETATE PH 4, ABOUT 10 MM CELLOBIOSE. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.979 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 20, 2010 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.78→30 Å / Num. obs: 23941 / % possible obs: 99.4 % / Observed criterion σ(I): 2 / Redundancy: 7.1 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 5.7 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: UNPUBLISHED WILD TYPE CEL6B Resolution: 2→46.2 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.93 / SU B: 3.532 / SU ML: 0.1 / Cross valid method: THROUGHOUT / ESU R: 0.203 / ESU R Free: 0.16 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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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: 14.171 Å2
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Refinement step | Cycle: LAST / Resolution: 2→46.2 Å
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Refine LS restraints |
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