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- PDB-3cel: ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3cel | ||||||||||||
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Title | ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE | ||||||||||||
![]() | 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I | ||||||||||||
![]() | HYDROLASE / CELLULOSE DEGRADATION / GLYCOSIDASE / GLYCOPROTEIN | ||||||||||||
Function / homology | ![]() cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() | ||||||||||||
![]() | Divne, C. / Stahlberg, J. / Jones, T.A. | ||||||||||||
![]() | ![]() Title: Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. Authors: Stahlberg, J. / Divne, C. / Koivula, A. / Piens, K. / Claeyssens, M. / Teeri, T.T. / Jones, T.A. #1: ![]() Title: The Three-Dimensional Crystal Structure of the Catalytic Core of Cellobiohydrolase I from Trichoderma Reesei Authors: Divne, C. / Stahlberg, J. / Reinikainen, T. / Ruohonen, L. / Pettersson, G. / Knowles, J.K. / Teeri, T.T. / Jones, T.A. #2: ![]() Title: Crystallization and Preliminary X-Ray Studies on the Core Proteins of Cellobiohydrolase I and Endoglucanase I from Trichoderma Reesei Authors: Divne, C. / Sinning, I. / Stahlberg, J. / Pettersson, G. / Bailey, M. / Siika-Aho, M. / Margolles-Clark, E. / Teeri, T. / Jones, T.A. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91 KB | Display | ![]() |
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PDB format | ![]() | 72.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 724.6 KB | Display | ![]() |
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Full document | ![]() | 724.4 KB | Display | |
Data in XML | ![]() | 18.9 KB | Display | |
Data in CIF | ![]() | 27.7 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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 46067.754 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 1 - 434 / Mutation: E212Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P00725, UniProt: P62694*PLUS, cellulose 1,4-beta-cellobiosidase (non-reducing end) | ||||||
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#2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellobiose | ||||||
#3: Sugar | ChemComp-NAG / | ||||||
#4: Chemical | ChemComp-CD / #5: Water | ChemComp-HOH / | Compound details | THE I222 CRYSTAL FORM DESCRIBED HERE REPRESENTS THE HIGHER SYMMETRY EQUIVALENT TO THE PSEUDO-I222 ...THE I222 CRYSTAL FORM DESCRIBED HERE REPRESENTS | Nonpolymer details | THERE IS A CADMIUM (+II) COUNTER ION COORDINATED BY GLU 295 AND GLU 325 FROM ONE MOLECULE, TOGETHER ...THERE IS A CADMIUM (+II) COUNTER ION COORDINATE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 Details: 50 MM MES PH 6.0, 5% MONOMETHYL ETHER PEG 5000, 5 MM CDCL2, 1 MM CELLOBIOSE | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: May 6, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→67.1 Å / Num. obs: 26782 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Rmerge(I) obs: 0.077 / Net I/σ(I): 5.4 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.148 / Mean I/σ(I) obs: 4.1 / % possible all: 99.4 |
Reflection | *PLUS Num. measured all: 138916 |
Reflection shell | *PLUS % possible obs: 99.4 % |
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Processing
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Refinement | Resolution: 2→7.5 Å / σ(F): 0
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Displacement parameters | Biso mean: 17.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→7.5 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: STRICT NCS CONSTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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