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Open data
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Basic information
Entry | Database: PDB / ID: 4im4 | ||||||
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Title | Multifunctional cellulase, xylanase, mannanase | ||||||
![]() | Endoglucanase E | ||||||
![]() | HYDROLASE / cellulase / xylanase / mannanase / multifunction / Endo-1 / 4-beta-glucanase / biomass degradation | ||||||
Function / homology | ![]() glucomannan catabolic process / acetylxylan esterase / acetylxylan esterase activity / Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases / cellulose binding / cellulase / cellulase activity / xylan catabolic process / cellulose catabolic process / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Bianchetti, C.M. / Takasuka, T.E. / Fox, B.G. | ||||||
![]() | ![]() Title: A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis. Authors: Glasgow, E.M. / Kemna, E.I. / Bingman, C.A. / Ing, N. / Deng, K. / Bianchetti, C.M. / Takasuka, T.E. / Northen, T.R. / Fox, B.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 425.4 KB | Display | ![]() |
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PDB format | ![]() | 348.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 462.5 KB | Display | ![]() |
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Full document | ![]() | 482.3 KB | Display | |
Data in XML | ![]() | 82.2 KB | Display | |
Data in CIF | ![]() | 118.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6mq4C ![]() 6pz7C ![]() 6q1iC ![]() 6ui3C ![]() 6wqpC ![]() 6wqvC ![]() 6wqyC ![]() 6xrkC ![]() 6xsoC ![]() 6xsuC ![]() 3ndyS ![]() 4im1 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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Unit cell |
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Components
#1: Protein | Mass: 38185.832 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.27 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: Protein Solution (20 mg/ml protein, 0.05 M NaCl, 0.010 M MOPS pH 7.0) mixed in a 1:1 ratio with the Well Solution (9% PEG 20,000, 18% mmPEG 550,0.3 M diethyleneglycol, 0.3 M ...Details: Protein Solution (20 mg/ml protein, 0.05 M NaCl, 0.010 M MOPS pH 7.0) mixed in a 1:1 ratio with the Well Solution (9% PEG 20,000, 18% mmPEG 550,0.3 M diethyleneglycol, 0.3 M triethyleneglycol, 0.3 M tetraethyleneglycol, 0.3 M pentaethyleneglycol, 100mM MES/Imidazole buffer pH 6.5). Cryoprotected with 9% PEG 20,000, 18% mmPEG 550, 0.3 M diethyleneglycol, 0.3 M triethyleneglycol, 0.3 M tetraethyleneglycol, 0.3 M pentaethyleneglycol, 100mM MES/Imidazole buffer pH 6.5, 15% ethylene glycol, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 10, 2012 / Details: mirrors and beryllium lenses | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.42→50 Å / Num. obs: 92255 / % possible obs: 99.6 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.193 / Χ2: 0.92 / Net I/σ(I): 3.6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 3NDY Resolution: 2.42→47.352 Å / Occupancy max: 1 / Occupancy min: 0.13 / SU ML: 0.32 / σ(F): 1.34 / Phase error: 27.09 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 67.2 Å2 / Biso mean: 14.6576 Å2 / Biso min: 1.66 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.42→47.352 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14
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