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Yorodumi- PDB-1v0a: Family 11 Carbohydrate-Binding Module of cellulosomal cellulase L... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v0a | ||||||
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Title | Family 11 Carbohydrate-Binding Module of cellulosomal cellulase Lic26A-Cel5E of Clostridium thermocellum | ||||||
Components | ENDOGLUCANASE H | ||||||
Keywords | HYDROLASE / CARBOHYDRATE BINDING MODULE / CELLULOSOME / CLOSTRIDIUM THERMOCELLUM / CELLULOSE DEGRADATION / GLYCOSIDASE | ||||||
Function / homology | Function and homology information | ||||||
Biological species | CLOSTRIDIUM THERMOCELLUM (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.98 Å | ||||||
Authors | Carvalho, A.L. / Romao, M.J. / Goyal, A. / Prates, J.A.M. / Pires, V.M.R. / Ferreira, L.M.A. / Bolam, D.N. / Gilbert, H.J. / Fontes, C.M.G.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: The Family 11 Carbohydrate-Binding Module of Clostridium Thermocellum Lic26A-Cel5E Accomodates Beta-1,4- and Beta-1,3-1,4-Mixed Linked Glucans at a Single Binding Site Authors: Carvalho, A.L. / Goyal, A. / Prates, J.A.M. / Bolam, D.N. / Gilbert, H.J. / Pires, V.M.R. / Ferreira, L.M.A. / Planas, A. / Romao, M.J. / Fontes, C.M.G.A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v0a.cif.gz | 48.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v0a.ent.gz | 37.3 KB | Display | PDB format |
PDBx/mmJSON format | 1v0a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/1v0a ftp://data.pdbj.org/pub/pdb/validation_reports/v0/1v0a | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20073.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CLOSTRIDIUM THERMOCELLUM (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P16218, cellulase | ||||||
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#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-GLUCOSIDIC LINKAGES IN CELLULOSE, LICHENIN AND ...CATALYTIC ACTIVITY: ENDOHYDROL | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 36.5 % |
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Crystal grow | pH: 6 / Details: pH 6.00 |
-Data collection
Diffraction | Mean temperature: 110 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.981033,0.981266, 0.976315 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.977→24.299 Å / Num. obs: 11449 / % possible obs: 99.5 % / Redundancy: 1.84 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 30.3 | ||||||||||||
Reflection shell | Resolution: 1.98→2.02 Å / Rmerge(I) obs: 0.099 / Mean I/σ(I) obs: 8.4 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.98→19 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.902 / SU B: 3.961 / SU ML: 0.113 / Cross valid method: THROUGHOUT / ESU R: 0.225 / ESU R Free: 0.177 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.6 Å2
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Refinement step | Cycle: LAST / Resolution: 1.98→19 Å
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Refine LS restraints |
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