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Yorodumi- PDB-4x0v: Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 -
+Open data
-Basic information
Entry | Database: PDB / ID: 4x0v | ||||||
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Title | Structure of a GH5 family lichenase from Caldicellulosiruptor sp. F32 | ||||||
Components | Beta-1,3-1,4-glucanaseEndo-1,3(4)-b-glucanase | ||||||
Keywords | HYDROLASE / GLYCOSIDASE / LICHENASE | ||||||
Function / homology | Function and homology information organic substance metabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds Similarity search - Function | ||||||
Biological species | Caldicellulosiruptor sp. F32 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.798 Å | ||||||
Authors | Meng, D. / Liu, X. / Wang, X. / Li, F. / Feng, Y. | ||||||
Citation | Journal: Biochem. J. / Year: 2017 Title: Structural Insights into the Substrate Specificity of a Glycoside Hydrolase Family 5 Lichenase from Caldicellulosiruptor sp. F32 Authors: Meng, D.D. / Liu, X. / Dong, S. / Wang, Y.F. / Ma, X.Q. / Zhou, H. / Wang, X. / Yao, L.S. / Feng, Y. / Li, F.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4x0v.cif.gz | 590.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4x0v.ent.gz | 489.7 KB | Display | PDB format |
PDBx/mmJSON format | 4x0v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x0/4x0v ftp://data.pdbj.org/pub/pdb/validation_reports/x0/4x0v | HTTPS FTP |
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-Related structure data
Related structure data | 5h4rC 1edgS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
-Components
#1: Protein | Mass: 45883.039 Da / Num. of mol.: 8 / Fragment: UNP residues 24-401 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caldicellulosiruptor sp. F32 (bacteria) Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: R9RX81, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.51 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2 M Li citrate tribasic, 20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å |
Detector | Type: RIGAKU / Detector: CCD / Date: Oct 30, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.798→50 Å / Num. obs: 78399 / % possible obs: 99.8 % / Redundancy: 3.7 % / Net I/σ(I): 11.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1EDG Resolution: 2.798→46.65 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 27.14 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.798→46.65 Å
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Refine LS restraints |
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LS refinement shell |
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