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Yorodumi- PDB-1cen: CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN COMPLEXED WI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cen | |||||||||
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Title | CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN COMPLEXED WITH CELLOHEXAOSE | |||||||||
Components | CELLULASE CELC | |||||||||
Keywords | CELLULOSE DEGRADATION / GLYCOSYL HYDROLASE / CELLULASE / FAMILY A/5 OF GLYCOSYL HYDROLASES / CLOSTRIDIUM THERMOCELLUM | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Clostridium thermocellum (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | |||||||||
Authors | Dominguez, R. / Alzari, P.M. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. Authors: Dominguez, R. / Souchon, H. / Lascombe, M. / Alzari, P.M. #1: Journal: Nat.Struct.Biol. / Year: 1995 Title: A Common Protein Fold and Similar Active Site in Two Distinct Families of Beta-Glycanases Authors: Dominguez, R. / Souchon, H. / Spinelli, S. / Dauter, Z. / Wilson, K.S. / Chauvaux, S. / Beguin, P. / Alzari, P.M. #2: Journal: Biochem.Biophys.Res.Commun. / Year: 1992 Title: Site-Directed Mutagenesis of Conserved Residues of Clostridium Thermocellum Endoglucanase Celc Authors: Navas, J. / Beguin, P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cen.cif.gz | 86.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cen.ent.gz | 65.5 KB | Display | PDB format |
PDBx/mmJSON format | 1cen.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/1cen ftp://data.pdbj.org/pub/pdb/validation_reports/ce/1cen | 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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Atom site foot note | 1: CIS PROLINE - PRO 202 / 2: CIS PROLINE - PRO 226 3: TRP 313 - ASN 314 OMEGA = 0.12 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-Components
#1: Protein | Mass: 40947.352 Da / Num. of mol.: 1 / Mutation: E140Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium thermocellum (bacteria) / Strain: NCIB 10682 / Plasmid: PCT306 (PUC9) / Production host: Escherichia coli (E. coli) References: UniProt: P07985, UniProt: P0C2S3*PLUS, cellulase |
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#2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellobiose |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.87 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.2 / Method: unknown | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.927 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.927 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 16218 / % possible obs: 94.1 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.089 |
Reflection | *PLUS Num. measured all: 105099 / Rmerge(I) obs: 0.089 |
-Processing
Software |
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Refinement | Resolution: 2.3→10 Å
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Displacement parameters | Biso mean: 20.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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