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Yorodumi- PDB-6pz7: GH5-4 broad specificity endoglucanase from Clostridium acetobutylicum -
+Open data
-Basic information
Entry | Database: PDB / ID: 6pz7 | ||||||
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Title | GH5-4 broad specificity endoglucanase from Clostridium acetobutylicum | ||||||
Components | Endoglucanase family 5 | ||||||
Keywords | HYDROLASE / GH5-4 / endoglucanase / GLBRC | ||||||
Function / homology | Glycoside hydrolase, family 5, conserved site / Glycosyl hydrolases family 5 signature. / Glycoside hydrolase, family 5 / Cellulase (glycosyl hydrolase family 5) / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / Glycoside hydrolase superfamily / Endoglucanase family 5 Function and homology information | ||||||
Biological species | Clostridium acetobutylicum ATCC 824 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.25 Å | ||||||
Authors | Bianchetti, C.M. / Bingman, C.A. / Fox, B.G. | ||||||
Funding support | United States, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2020 Title: A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis. Authors: Glasgow, E.M. / Kemna, E.I. / Bingman, C.A. / Ing, N. / Deng, K. / Bianchetti, C.M. / Takasuka, T.E. / Northen, T.R. / Fox, B.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6pz7.cif.gz | 256.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6pz7.ent.gz | 171 KB | Display | PDB format |
PDBx/mmJSON format | 6pz7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pz/6pz7 ftp://data.pdbj.org/pub/pdb/validation_reports/pz/6pz7 | HTTPS FTP |
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-Related structure data
Related structure data | 4im4C 6mq4C 6q1iC 6ui3C 6wqpC 6wqvC 6wqyC 6xrkC 6xsoC 6xsuC 3ndzS 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: 37301.551 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium acetobutylicum ATCC 824 (bacteria) Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 Gene: CA_C0826 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q97KU0 | ||||||
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#2: Chemical | #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 34.65 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5 Details: Protein was crystallized in SD2 plates set by a Mosquito crystallization robot. The hit came from PACT Premiere Screen A7, 200 mM NaCl, 100 mM sodium acetate pH 5.0, 25% PEG 6K. Crystals ...Details: Protein was crystallized in SD2 plates set by a Mosquito crystallization robot. The hit came from PACT Premiere Screen A7, 200 mM NaCl, 100 mM sodium acetate pH 5.0, 25% PEG 6K. Crystals were cryopreserved in reservoir solution supplemented with 15% ethylene glycol. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.97856 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 13, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→28.65 Å / Num. obs: 78485 / % possible obs: 95.1 % / Observed criterion σ(I): -3 / Redundancy: 7.3 % / Biso Wilson estimate: 9.83 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.0649 / Rpim(I) all: 0.02472 / Rrim(I) all: 0.06959 / Net I/σ(I): 19.11 |
Reflection shell | Resolution: 1.25→1.295 Å / Rmerge(I) obs: 0.2093 / Mean I/σ(I) obs: 4.41 / Num. unique obs: 5788 / CC1/2: 0.955 / Rpim(I) all: 0.1166 / Rrim(I) all: 0.2412 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3NDZ Resolution: 1.25→28.64 Å / SU ML: 0.0827 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 12.8069
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.45 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.25→28.64 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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