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Open data
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Basic information
Entry | Database: PDB / ID: 1ceo | ||||||
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Title | CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN | ||||||
![]() | CELLULASE CELC | ||||||
![]() | CELLULOSE DEGRADATION / GLYCOSYL HYDROLASE / CELLULASE / FAMILY A/5 OF GLYCOSYL HYDROLASES / CLOSTRIDIUM THERMOCELLUM | ||||||
Function / homology | ![]() cellulase / cellulase activity / beta-glucosidase activity / cellulose catabolic process / cell surface / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Dominguez, R. / Alzari, P.M. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.4 KB | Display | ![]() |
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PDB format | ![]() | 65.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 364.1 KB | Display | ![]() |
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Full document | ![]() | 366.7 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 13.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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 = 1.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 40947.352 Da / Num. of mol.: 1 / Mutation: E140Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P07985, UniProt: P0C2S3*PLUS, cellulase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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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: 1.8→50 Å / Num. obs: 34277 / % possible obs: 97.8 % / Redundancy: 5.7 % / Rmerge(I) obs: 0.086 |
Reflection | *PLUS Num. measured all: 195009 / Rmerge(I) obs: 0.086 |
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Processing
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Refinement | Resolution: 1.9→10 Å
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Displacement parameters | Biso mean: 25.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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