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- PDB-1h6x: The role of conserved amino acids in the cleft of the C-terminal ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1h6x | ||||||
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Title | The role of conserved amino acids in the cleft of the C-terminal family 22 carbohydrate binding module of Clostridium thermocellum Xyn10B in ligand binding | ||||||
![]() | ENDO-1,4-BETA-XYLANASE Y | ||||||
![]() | HYDROLASE / XYLAN DEGRADATION / GLYCOSIDASE | ||||||
Function / homology | ![]() cellulosome / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Xie, H. / Bolam, D.N. / Charnock, S.J. / Davies, G.J. / Williamson, M.P. / Simpson, P.J. / Fontes, C.M.G.A. / Ferreira, L.M.A. / Gilbert, H.J. | ||||||
![]() | ![]() Title: Clostridium Thermocellum Xyn10B Carbohydrate-Binding Module 22-2: The Role of Conserved Amino Acids in Ligand Binding Authors: Xie, H. / Gilbert, H.J. / Charnock, S.J. / Davies, G.J. / Williamson, M.P. / Simpson, P.J. / Raghothama, S. / Fontes, C.M.G.A. / Dias, F.M. / Ferreira, L.M.A. / Bolam, D.N. #1: ![]() Title: The X6 "Thermostabilizing" Domains of Xylanases are Carbohydrate-Binding Modules:Structure and Biochemistry of the Clostridium Thermocellum X6B Domain Authors: Charnock, S.J. / Bolam, D.N. / Turkenburg, J.P. / Gilbert, H.J. / Ferreira, L.M.A. / Davies, G.J. / Fontes, C.M.G.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 46.9 KB | Display | ![]() |
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PDB format | ![]() | 32.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 414.6 KB | Display | ![]() |
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Full document | ![]() | 415.5 KB | Display | |
Data in XML | ![]() | 9.4 KB | Display | |
Data in CIF | ![]() | 12.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h6yC ![]() 1dyoS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 18911.768 Da / Num. of mol.: 1 / Fragment: XYLAN BINDING DOMAIN RESIDUE 560-720 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
Compound details | CHAIN A ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.07 % | |||||||||||||||
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Crystal grow | pH: 7 / Details: 1.7 M AMMONIUM SULPHATE, pH 7.00 | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 15, 2000 / Details: FOCUSING AND MULTILAYER |
Radiation | Monochromator: G2(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→15 Å / Num. obs: 8438 / % possible obs: 98 % / Observed criterion σ(I): 3 / Redundancy: 7.21 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 29.7 |
Reflection shell | Resolution: 2.25→2.33 Å / Redundancy: 6.35 % / Rmerge(I) obs: 0.367 / Mean I/σ(I) obs: 4.83 / % possible all: 97 |
Reflection | *PLUS Lowest resolution: 15 Å / % possible obs: 98 % |
Reflection shell | *PLUS % possible obs: 97 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DYO Resolution: 2.25→15 Å / Cross valid method: THROUGHOUT / σ(F): 3
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Refinement step | Cycle: LAST / Resolution: 2.25→15 Å
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Refinement | *PLUS Lowest resolution: 15 Å / Rfactor Rfree: 0.257 / Rfactor Rwork: 0.204 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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