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- PDB-1cec: A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cec | ||||||
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Title | A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES | ||||||
![]() | ENDOGLUCANASE CELC | ||||||
![]() | HYDROLASE (GLYCOSYL) / GLYCOSYL HYDROLASE / CELLULASE / FAMILY A/5 OF CELLULASES/GLYCOSYL HYDROLASES / CLOSTRIDIUM THERMOCELLUM / ENDOGLUCANASE C | ||||||
Function / homology | ![]() cellulase / cellulase activity / beta-glucosidase activity / cellulose catabolic process / cell surface / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Alzari, P.M. / Dominguez, R. | ||||||
![]() | ![]() 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. #1: ![]() Title: Characterization of Two Crystal Forms of Clostridium Thermocellum Endoglucanase Celc Authors: Dominguez, R. / Souchon, H. / Alzari, P.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.1 KB | Display | ![]() |
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PDB format | ![]() | 63 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 364.8 KB | Display | ![]() |
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Full document | ![]() | 367.2 KB | Display | |
Data in XML | ![]() | 7.8 KB | Display | |
Data in CIF | ![]() | 12.3 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 = 1.73 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 40948.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: CELLULASE FAMILY A/5 / 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 Temperature: 24 ℃ / pH: 7.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
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: Nov 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 19891 / % possible obs: 90.7 % / Redundancy: 7.6 % / Rmerge(I) obs: 0.086 |
Reflection | *PLUS Highest resolution: 2.15 Å / Lowest resolution: 20 Å / Rmerge(I) obs: 0.086 |
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Processing
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Refinement | Resolution: 2.15→6 Å / σ(F): 3
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Displacement parameters | Biso mean: 31.51 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→6 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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