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Yorodumi- PDB-1f9d: Crystal structure of the cellulase CEL48F from C. cellulolyticum ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f9d | |||||||||
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Title | Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellotetraose | |||||||||
Components | ENDO-1,4-BETA-GLUCANASE F | |||||||||
Keywords | HYDROLASE / Cellulase / Protein-Cellotetraose Complex | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Clostridium cellulolyticum (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | |||||||||
Authors | Parsiegla, G. / Reverbel-Leroy, C. / Tardif, C. / Belaich, J.P. / Driguez, H. / Haser, R. | |||||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Crystal Structures of the Cellulase Cel48F in Complex with Inhibitors and Substrates Give Insights Into its Processive Action Authors: Parsiegla, G. / Reverbel-Leroy, C. / Tardif, C. / Belaich, J.P. / Driguez, H. / Haser, R. #1: Journal: Embo J. / Year: 1998 Title: The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A Authors: Parsiegla, G. / Juy, M. / Reverbel-Leroy, C. / Tardif, C. / Belaich, C. / Driguez, H. / Haser, R. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f9d.cif.gz | 142.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f9d.ent.gz | 111.2 KB | Display | PDB format |
PDBx/mmJSON format | 1f9d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f9/1f9d ftp://data.pdbj.org/pub/pdb/validation_reports/f9/1f9d | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 70868.891 Da / Num. of mol.: 1 / Fragment: CATALYTIC MODULE / Mutation: E55Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium cellulolyticum (bacteria) / Plasmid: PETF55 / Organelle (production host): BL21 DE3 / Production host: Escherichia coli (E. coli) / References: UniProt: P37698, cellulase |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D- ...alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltopentaose |
#3: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltotetraose |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.88 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 4000, HEPES, calcium chloride, Cellotetraose, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 14, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.28→54.8 Å / Num. all: 217505 / Num. obs: 29629 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 7.3 % / Biso Wilson estimate: 27.4 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 6.3 |
Reflection shell | Resolution: 2.28→2.36 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.377 / Num. unique all: 2843 / % possible all: 99.5 |
Reflection shell | *PLUS % possible obs: 99.5 % / Mean I/σ(I) obs: 2 |
-Processing
Software |
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Refinement | Resolution: 2.3→54.8 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→54.8 Å
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Refine LS restraints |
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