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Yorodumi- PDB-6to0: Structure of E70A mutant of Rex8A from Paenibacillus barcinonensi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6to0 | |||||||||
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Title | Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 2(3)-alpha-L-arabinofuranosyl-xylotriose. | |||||||||
Components | Reducing-end xylose-releasing exo-oligoxylanase Rex8A | |||||||||
Keywords | HYDROLASE / Xylan / Exo-oligoxylanase / Xylanases / Xylooligosaccharides / Xylooligomers / Xylose / Hydrolysis / Polysaccharides / Glycan / Glycan degradation / Xylan degradation / Glycosidase / Carbohydrate metabolism. | |||||||||
Function / homology | Function and homology information oligosaccharide reducing-end xylanase / oligosaccharide reducing-end xylanase activity / xylan catabolic process Similarity search - Function | |||||||||
Biological species | Paenibacillus barcinonensis (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.88 Å | |||||||||
Authors | Jimenez-Ortega, E. / Ramirez-Escudero, M. / Sanz-Aparicio, J. | |||||||||
Citation | Journal: Febs J. / Year: 2020 Title: Structural analysis of the reducing-end xylose-releasing exo-oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 deciphers its molecular specificity. Authors: Jimenez-Ortega, E. / Valenzuela, S. / Ramirez-Escudero, M. / Pastor, F.J. / Sanz-Aparicio, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6to0.cif.gz | 175.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6to0.ent.gz | 138.7 KB | Display | PDB format |
PDBx/mmJSON format | 6to0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/to/6to0 ftp://data.pdbj.org/pub/pdb/validation_reports/to/6to0 | HTTPS FTP |
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-Related structure data
Related structure data | 6shyC 6srdSC 6sudC 6towC 6tppC 6trhC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 0 / Auth seq-ID: 6 - 385 / Label seq-ID: 6 - 385
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-Components
#1: Protein | Mass: 44678.430 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Paenibacillus barcinonensis (bacteria) / Gene: rex8A, DFQ00_11062 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: A0A0S2UQQ5, oligosaccharide reducing-end xylanase #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.53 Å3/Da / Density % sol: 65 % / Description: Bar |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 18% PEG 3350, 0.2M Potassium thiocyanate, 0.1M Bis-Tris propane pH 7.5. Microseeding. Co-crystallization with 2(3)-alpha-L-arabinofuranosyl-xylotriose |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.97926 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 20, 2019 / Details: KB Mirrors |
Radiation | Monochromator: Si(111) channel-cut, cryocooled / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97926 Å / Relative weight: 1 |
Reflection | Resolution: 1.88→44.53 Å / Num. obs: 100926 / % possible obs: 99.9 % / Redundancy: 6.5 % / CC1/2: 0.998 / Rmerge(I) obs: 0.078 / Rpim(I) all: 0.032 / Rrim(I) all: 0.085 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.88→1.91 Å / Rmerge(I) obs: 0.609 / Num. unique obs: 4930 / CC1/2: 0.92 / Rpim(I) all: 0.357 / Rrim(I) all: 0.66 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6SRD Resolution: 1.88→44.53 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.906 / SU B: 3.271 / SU ML: 0.097 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.141 / ESU R Free: 0.131 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 88.11 Å2 / Biso mean: 27.956 Å2 / Biso min: 17.62 Å2
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Refinement step | Cycle: final / Resolution: 1.88→44.53 Å
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Refine LS restraints |
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Refine LS restraints NCS | Ens-ID: 1 / Number: 14065 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.05 Å / Weight position: 0.05
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LS refinement shell | Resolution: 1.88→1.929 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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