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- PDB-6fkx: Crystal structure of an acetyl xylan esterase from a desert metagenome -
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Open data
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Basic information
Entry | Database: PDB / ID: 6fkx | ||||||
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Title | Crystal structure of an acetyl xylan esterase from a desert metagenome | ||||||
![]() | (Acetyl xylan ...) x 3 | ||||||
![]() | HYDROLASE / Carbohydrate-active enzyme / acetyl xylan esterase / alpha-beta hydrolase / 7-ACA deacetylase | ||||||
Function / homology | Alpha/Beta hydrolase fold, catalytic domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / FORMIC ACID![]() | ||||||
Biological species | metagenome (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Adesioye, F.A. / Makhalanyane, T.P. / Vikram, S. / Sewell, B.T. / Schubert, W. / Cowan, D.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Characterization and Directed Evolution of a Novel Acetyl Xylan Esterase Reveals Thermostability Determinants of the Carbohydrate Esterase 7 Family. Authors: Adesioye, F.A. / Makhalanyane, T.P. / Vikram, S. / Sewell, B.T. / Schubert, W.D. / Cowan, D.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 | ![]() | 795.4 KB | Display | ![]() |
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PDB format | ![]() | 646.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3fcyS 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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Unit cell |
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Components
-Acetyl xylan ... , 3 types, 6 molecules ABDEFC
#1: Protein | Mass: 36036.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Namib Desert Soil Hypolith / Source: (gene. exp.) metagenome (others) / Plasmid: pET28a / Details (production host): Circular with 6X His-tags / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 35760.395 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Namib Desert Soil Hypolith / Source: (gene. exp.) metagenome (others) / Plasmid: pET28a / Details (production host): Circular 6X His-tag / Production host: ![]() ![]() #3: Protein | | Mass: 35426.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Namib Desert Soil Hypolith / Source: (gene. exp.) metagenome (others) / Plasmid: pET28a / Details (production host): Circular, 6X His-tag / Production host: ![]() ![]() |
-Non-polymers , 5 types, 2285 molecules ![](data/chem/img/NA.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-NA / #5: Chemical | ChemComp-MES / #6: Chemical | ChemComp-SO4 / | #7: Chemical | ChemComp-FMT / | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.38 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.1 M 2-(N-morpholino) ethanesulfonic acid (MES) buffers pH 8.5 and 25% PEG 8000 (w/v) PH range: 6.5-8.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 9, 2016 |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.972 Å / Relative weight: 1 |
Reflection | Resolution: 2.026→89.23 Å / Num. obs: 130734 / % possible obs: 99.95 % / Redundancy: 2 % / Rmerge(I) obs: 0.06564 / Rpim(I) all: 0.06564 / Rrim(I) all: 0.09283 / Net I/σ(I): 10.02 |
Reflection shell | Resolution: 2.026→2.099 Å / Rmerge(I) obs: 0.3479 / Rpim(I) all: 0.3479 / Rrim(I) all: 0.4921 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3FCY Resolution: 2.03→89.23 Å / Cross valid method: FREE R-VALUE
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Refinement step | Cycle: LAST / Resolution: 2.03→89.23 Å
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