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Yorodumi- PDB-4v1z: The 3-D structure of the cellobiohydrolase, Cel7A, from Aspergill... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4v1z | |||||||||
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Title | The 3-D structure of the cellobiohydrolase, Cel7A, from Aspergillus fumigatus | |||||||||
Components | CELLOBIOHYDROLASE | |||||||||
Keywords | HYDROLASE / CELLULASE / BIOFUELS / CARBOHYDRATE-ACTIVE ENZYME / THERMAL 2 STABILITY | |||||||||
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 | ASPERGILLUS FUMIGATUS (mold) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.78 Å | |||||||||
Authors | Moroz, O.V. / Maranta, M. / Shaghasi, T. / Harris, P.V. / Wilson, K.S. / Davies, G.J. | |||||||||
Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2015 Title: The Three-Dimensional Structure of the Cellobiohydrolase Cel7A from Aspergillus Fumigatus at 1.5 A Resolution Authors: Moroz, O.V. / Maranta, M. / Shaghasi, T. / Harris, P.V. / Wilson, K.S. / Davies, G.J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v1z.cif.gz | 110.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4v1z.ent.gz | 84 KB | Display | PDB format |
PDBx/mmJSON format | 4v1z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v1/4v1z ftp://data.pdbj.org/pub/pdb/validation_reports/v1/4v1z | HTTPS FTP |
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-Related structure data
Related structure data | 4v20C 1q9hS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 47137.566 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 27-466 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ASPERGILLUS FUMIGATUS (mold) / Production host: ASPERGILLUS ORYZAE (mold) References: UniProt: Q4WM08, cellulose 1,4-beta-cellobiosidase (non-reducing end) | ||
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#2: Sugar | ChemComp-NAG / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51 % / Description: NONE |
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Crystal grow | Details: PACT B12 20% PEG6K, 10 MM ZNCL2, MES PH 6.0, OPTIMIZED MANUALLY |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Type: DIAMOND / Wavelength: 0.98 |
Detector | Date: Jul 11, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.78→65.69 Å / Num. obs: 44036 / % possible obs: 99.3 % / Observed criterion σ(I): 2 / Redundancy: 5.9 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 1.78→1.88 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 2.9 / % possible all: 98.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1Q9H Resolution: 1.78→67.85 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.957 / SU B: 2.485 / SU ML: 0.074 / Cross valid method: THROUGHOUT / ESU R: 0.097 / ESU R Free: 0.102 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.699 Å2
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Refinement step | Cycle: LAST / Resolution: 1.78→67.85 Å
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Refine LS restraints |
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