+Open data
-Basic information
Entry | Database: PDB / ID: 6cel | ||||||||||||
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Title | CBH1 (E212Q) CELLOPENTAOSE COMPLEX | ||||||||||||
Components | 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I | ||||||||||||
Keywords | HYDROLASE / CELLULOSE DEGRADATION / GLYCOSIDASE / GLYCOPROTEIN / GLYCOSYLATED PROTEIN | ||||||||||||
Function / homology | Function and homology information 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 | Hypocrea jecorina (fungus) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.7 Å | ||||||||||||
Authors | Divne, C. / Stahlberg, J. / Jones, T.A. | ||||||||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. Authors: Divne, C. / Stahlberg, J. / Teeri, T.T. / Jones, T.A. #1: Journal: J.Mol.Biol. / Year: 1996 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. #2: Journal: Science / Year: 1994 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. #3: Journal: J.Mol.Biol. / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6cel.cif.gz | 107 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6cel.ent.gz | 84.9 KB | Display | PDB format |
PDBx/mmJSON format | 6cel.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/6cel ftp://data.pdbj.org/pub/pdb/validation_reports/ce/6cel | 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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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#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.) Hypocrea jecorina (fungus) / Strain: QM 9414 / Gene: CBH1 / Variant: VTT-D-93201 / Plasmid: PEM-F5 / Gene (production host): CBH1 / Production host: Hypocrea jecorina (fungus) References: UniProt: P00725, UniProt: P62694*PLUS, cellulose 1,4-beta-cellobiosidase (non-reducing end) |
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-Sugars , 3 types, 4 molecules
#2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellotetraose |
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#3: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D- ...beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellopentaose |
#4: Sugar |
-Non-polymers , 2 types, 487 molecules
#5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Compound details | THE COORDINATES GIVEN DEFINE THE STRUCTURE OF ONLY THE CATALYTIC DOMAIN (RESIDUES 1 - 434) OF THE ...THE COORDINATE |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6 Details: HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK ...Details: HANGING DROPS. EQUAL VOLUMES OF 8 MG/ML PROTEIN AND RESERVOIR SOLUTION CONTAINING 0.1 M MES (PH 6.0), 18% MONOMETHYL ETHER PEG 5000, 0.01 M COCL2, AND 0.02% NA-AZIDE. CRYOPROTECTANT/SOAK SOLUTION CONTAINED 0.1 M MES (PH 6.0), 20% (W/V) MONOMETHYLETHER PEG 5000, 0.01 M COCL2, 15% GLYCEROL AND 0.004 M CELLOTETRAOSE. THE AXES OF THE CRYO-COOLED CRYSTALS ARE SYSTEMATICALLY SHORTER THAN THOSE OF CRYSTALS COLLECTED AT ROOM TEMPERATURE. IN ORDER TO KEEP THE SAME INDEXING AS IN PREVIOUS ROOM-TEMPERATURE DATA SETS, THE LONGER A-AXIS IS LISTED BEFORE THE SHORTER B-AXIS., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.862 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 31, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.862 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→65.9 Å / Num. obs: 42894 / % possible obs: 93.5 % / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Rmerge(I) obs: 0.083 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 1.65→1.69 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.408 / Mean I/σ(I) obs: 1.8 / % possible all: 90.9 |
Reflection shell | *PLUS % possible obs: 90.9 % |
-Processing
Software |
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Refinement | Resolution: 1.7→7.5 Å / σ(F): 0
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Displacement parameters | Biso mean: 9.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→7.5 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |