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- PDB-2w1w: Native structure of a family 35 carbohydrate binding module from ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2w1w | ||||||
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Title | Native structure of a family 35 carbohydrate binding module from Clostridium thermocellum | ||||||
![]() | LIPOLYTIC ENZYME, G-D-S-L | ||||||
![]() | HYDROLASE / FAMILY 35 / URONIC ACID SUGARS / CLOSTRIDIUM THERMOCELLUM / CARBOHYDRATE BINDING MODULE | ||||||
Function / homology | ![]() hydrolase activity, acting on ester bonds / polysaccharide catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gloster, T.M. / Davies, G.J. / Correia, M. / Prates, J. / Fontes, C. / Gilbert, H.J. | ||||||
![]() | ![]() Title: Evidence that Family 35 Carbohydrate Binding Modules Display Conserved Specificity But Divergent Function. Authors: Montanier, C. / Van Bueren, A.L. / Dumon, C. / Flint, J.E. / Correia, M.A. / Prates, J.A. / Firbank, S.J. / Lewis, R.J. / Grondin, G.G. / Ghinet, M.G. / Gloster, T.M. / Herve, C. / Knox, J.P. ...Authors: Montanier, C. / Van Bueren, A.L. / Dumon, C. / Flint, J.E. / Correia, M.A. / Prates, J.A. / Firbank, S.J. / Lewis, R.J. / Grondin, G.G. / Ghinet, M.G. / Gloster, T.M. / Herve, C. / Knox, J.P. / Talbot, B.G. / Turkenburg, J.P. / Kerovuo, J. / Brzezinski, R. / Fontes, C.M.G.A. / Davies, G.J. / Boraston, A.B. / Gilbert, H.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.9 KB | Display | ![]() |
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PDB format | ![]() | 104.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 457.2 KB | Display | ![]() |
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Full document | ![]() | 460.5 KB | Display | |
Data in XML | ![]() | 17.4 KB | Display | |
Data in CIF | ![]() | 26.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2vzpC ![]() 2vzqC ![]() 2vzrC ![]() 2w3jC ![]() 2w46C ![]() 2w47C ![]() 2w87C C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 15899.540 Da / Num. of mol.: 2 / Fragment: RESIDUES 479-613 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-PO4 / | #5: Water | ChemComp-HOH / | Sequence details | THE SECTION OF THE GENE CORRESPONDING TO RESIDUES 479-613 WAS CLONED. THE FIRST 3 RESIDUES AND LAST ...THE SECTION OF THE GENE CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 69 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: 0.1 M HEPES, PH 7.5, 0.8 M SODIUM PHOSPHATE MONOBASIC, 0.8 M POTASSIUM PHOSPHATE MONOBASIC |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 17, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0004 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→15 Å / Num. obs: 37854 / % possible obs: 99 % / Redundancy: 7.7 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 1.55→1.61 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 11.93 Å2
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Refinement step | Cycle: LAST / Resolution: 1.55→204.12 Å
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Refine LS restraints |
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