+Open data
-Basic information
Entry | Database: PDB / ID: 1fce | |||||||||
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Title | PROCESSIVE ENDOCELLULASE CELF OF CLOSTRIDIUM CELLULOLYTICUM | |||||||||
Components | CELLULASE CELF | |||||||||
Keywords | CELLULASE DEGRADATION / FAMILY 48 / THIOOLIGOSACCHARIDE INHIBITOR / PROCESSIVE ENDO ACTION / HYDROLASE | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Clostridium cellulolyticum (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / MIRAS / Resolution: 2 Å | |||||||||
Authors | Parsiegla, G. / Juy, M. / Haser, R. | |||||||||
Citation | 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 resolution. Authors: Parsiegla, G. / Juy, M. / Reverbel-Leroy, C. / Tardif, C. / Belaich, J.P. / 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 | 1fce.cif.gz | 180.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fce.ent.gz | 144 KB | Display | PDB format |
PDBx/mmJSON format | 1fce.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fc/1fce ftp://data.pdbj.org/pub/pdb/validation_reports/fc/1fce | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 70869.875 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium cellulolyticum (bacteria) / Cellular location: SECRETED ON CELLULOSOME / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P37698, cellulase | ||||
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#2: Polysaccharide | Type: oligosaccharide / Mass: 696.669 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-CA / | #4: 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: 2.2 Å3/Da / Density % sol: 45 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, hanging dropDetails: Reverbel-Leroy, C., (1997) Acta Crystallogr., D.54, 114. | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 43593 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4.2 % / Biso Wilson estimate: 18.5 Å2 / Rsym value: 0.073 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 3 / Rsym value: 0.248 / % possible all: 100 |
Reflection | *PLUS Rmerge(I) obs: 0.073 |
Reflection shell | *PLUS % possible obs: 100 % / Rmerge(I) obs: 0.248 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2→30 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 15.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Rfactor Rfree error: 0.004 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.163 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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