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- PDB-5l6f: Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5l6f | |||||||||
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Title | Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose | |||||||||
![]() | FAD linked oxidase-like protein | |||||||||
![]() | OXIDOREDUCTASE / FAD / CAZy / oligosaccharide / xylose / xylan | |||||||||
Function / homology | ![]() Oxidoreductases; Acting on the CH-OH group of donors; With oxygen as acceptor / FAD binding / oxidoreductase activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Rozeboom, H.J. / Ferrari, A.R. / Fraaije, M.W. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Discovery of a Xylooligosaccharide Oxidase from Myceliophthora thermophila C1. Authors: Ferrari, A.R. / Rozeboom, H.J. / Dobruchowska, J.M. / van Leeuwen, S.S. / Vugts, A.S. / Koetsier, M.J. / Visser, J. / Fraaije, M.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 208.7 KB | Display | ![]() |
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PDB format | ![]() | 165.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5k8eSC ![]() 5l6gC 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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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 54376.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: First 16 residues are a signal sequence Source: (gene. exp.) ![]() Gene: MYCTH_102971 Production host: ![]() References: UniProt: G2QG48, Oxidoreductases; Acting on the CH-OH group of donors; With oxygen as acceptor |
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-Sugars , 3 types, 9 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | beta-D-xylopyranose-(1-4)-beta-D-xylopyranose / 4beta-beta-xylobiose #5: Sugar | |
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-Non-polymers , 3 types, 402 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-FAD / |
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#6: Chemical | ChemComp-PEG / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 15-18% PEG3350, 0.1 M MES buffer, 0.2 M ammonium chloride |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 17, 2015 |
Radiation | Monochromator: HeliosMX mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→53.4 Å / Num. obs: 45931 / % possible obs: 99.4 % / Redundancy: 3.6 % / Biso Wilson estimate: 11.3 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.274 / Mean I/σ(I) obs: 3.3 / % possible all: 90 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5K8E Resolution: 1.8→53.4 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.951 / SU B: 4.644 / SU ML: 0.077 / Cross valid method: THROUGHOUT / ESU R: 0.113 / ESU R Free: 0.106 / 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: 1.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.848 Å2
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Refinement step | Cycle: 1 / Resolution: 1.8→53.4 Å
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Refine LS restraints |
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