+Open data
-Basic information
Entry | Database: PDB / ID: 1g9g | ||||||
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Title | XTAL-STRUCTURE OF THE FREE NATIVE CELLULASE CEL48F | ||||||
Components | CELLULASE CEL48F | ||||||
Keywords | HYDROLASE / Cellulase / processive-endo | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Clostridium cellulolyticum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Parsiegla, G. / Tardif, C. / Belaich, J.P. / Driguez, H. / Haser, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2008 Title: Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action Authors: Parsiegla, G. / Reverbel, C. / Tardif, C. / Driguez, H. / Haser, R. #1: 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. #2: Journal: Embo J. / Year: 1998 Title: The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thioligosaccharide 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 | 1g9g.cif.gz | 147.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g9g.ent.gz | 113.8 KB | Display | PDB format |
PDBx/mmJSON format | 1g9g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g9/1g9g ftp://data.pdbj.org/pub/pdb/validation_reports/g9/1g9g | HTTPS FTP |
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-Related structure data
Related structure data | 1g9jC 2qnoC 1fceS C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 70869.875 Da / Num. of mol.: 1 / Fragment: CATALYTIC MODULE Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium cellulolyticum (bacteria) / Plasmid: PETFC / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P37698, cellulase |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-MG / |
#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: 2.25 Å3/Da / Density % sol: 45.23 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: HEPES, PEG 4000, MgCl, Glucose, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K | |||||||||||||||||||||||||||||||||||
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: 290 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.9796 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 30, 1999 |
Radiation | Monochromator: Synchrotron / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→40 Å / Num. all: 54275 / Num. obs: 49813 / % possible obs: 98.2 % / Observed criterion σ(I): 2 / Redundancy: 3.8 % / Biso Wilson estimate: 12.7 Å2 / Rmerge(I) obs: 0.091 / Net I/σ(I): 6.8 |
Reflection shell | Resolution: 1.85→1.9 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.354 / Mean I/σ(I) obs: 1.9 / Num. unique all: 2584 / % possible all: 88.9 |
Reflection shell | *PLUS % possible obs: 88.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FCE Resolution: 1.9→38.59 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 2238873.49 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 36.74 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→38.59 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 1.85 Å / Lowest resolution: 40 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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