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- PDB-2vn5: The Clostridium cellulolyticum dockerin displays a dual binding m... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vn5 | ||||||
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Title | The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner | ||||||
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![]() | CELL ADHESION / CARBOHYDRATE METABOLISM / POLYSACCHARIDE DEGRADATION / COHESIN / DOCKERIN / HYDROLASE / CELLULOSOME / GLYCOSIDASE / CELLULOSE DEGRADATION | ||||||
Function / homology | ![]() hydrolase activity, acting on glycosyl bonds / cellulose binding / cellulase / cellulase activity / beta-glucosidase activity / cellulose catabolic process / cell surface / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pinheiro, B.A. / Prates, J.A.M. / Proctor, M.R. / Gilbert, H.J. / Davies, G.J. / Money, V.A. / Martinez-Fleites, C. / Bayer, E.A. / Fontes, C.M.G.A. / Fierobe, H.P. | ||||||
![]() | ![]() Title: The Clostridium Cellulolyticum Dockerin Displays a Dual Binding Mode for its Cohesin Partner. Authors: Pinheiro, B.A. / Proctor, M.R. / Martinez-Fleites, C. / Prates, J.A.M. / Money, V.A. / Davies, G.J. / Bayer, E.A. / Fontes, C.M.G.A. / Fierobe, H.P. / Gilbert, H.J. | ||||||
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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 93.2 KB | Display | ![]() |
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PDB format | ![]() | 71 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.9 KB | Display | ![]() |
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Full document | ![]() | 455 KB | Display | |
Data in XML | ![]() | 19.3 KB | Display | |
Data in CIF | ![]() | 28 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2vn6C ![]() 1ohzS C: citing same article ( S: Starting model for refinement |
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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
#1: Protein | Mass: 15557.599 Da / Num. of mol.: 2 / Fragment: RESIDUES 277-427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 7285.248 Da / Num. of mol.: 2 / Fragment: RESIDUES 410-475 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-CA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 39.64 % / Description: NONE |
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Crystal grow | Details: 0.2 M LITHIUM SULPHATE AND 25% W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 2000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 16, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 56370 / % possible obs: 98.5 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 19.4 |
Reflection shell | Resolution: 1.9→1.94 Å / Redundancy: 3 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 4.1 / % possible all: 94.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OHZ Resolution: 1.9→38.21 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.937 / SU B: 6.689 / SU ML: 0.102 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.161 / ESU R Free: 0.154 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.96 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→38.21 Å
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Refine LS restraints |
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