+Open data
-Basic information
Entry | Database: PDB / ID: 2wtn | ||||||
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Title | Ferulic Acid bound to Est1E from Butyrivibrio proteoclasticus | ||||||
Components | EST1E | ||||||
Keywords | HYDROLASE / ESTERASE / FERULIC ACID ESTERASE | ||||||
Function / homology | Function and homology information Peptidase S33 tripeptidyl aminopeptidase-like, C-terminal / TAP-like protein / Serine aminopeptidase, S33 / : / Serine aminopeptidase, S33 / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | CLOSTRIDIUM PROTEOCLASTICUM (bacteria) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 2.1 Å | ||||||
Authors | Goldstone, D.C. / Arcus, V.L. | ||||||
Citation | Journal: Proteins / Year: 2010 Title: Structural and Functional Characterization of a Promiscuous Feruloyl Esterase (Est1E) from the Rumen Bacterium Butyrivibrio Proteoclasticus. Authors: Goldstone, D.C. / Villas-Boas, S.G. / Till, M. / Kelly, W.J. / Attwood, G.T. / Arcus, V.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wtn.cif.gz | 114.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wtn.ent.gz | 88.7 KB | Display | PDB format |
PDBx/mmJSON format | 2wtn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2wtn_validation.pdf.gz | 473.2 KB | Display | wwPDB validaton report |
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Full document | 2wtn_full_validation.pdf.gz | 478.5 KB | Display | |
Data in XML | 2wtn_validation.xml.gz | 22.9 KB | Display | |
Data in CIF | 2wtn_validation.cif.gz | 32.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wt/2wtn ftp://data.pdbj.org/pub/pdb/validation_reports/wt/2wtn | HTTPS FTP |
-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
#1: Protein | Mass: 28057.234 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CLOSTRIDIUM PROTEOCLASTICUM (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: D2YW37*PLUS #2: Chemical | ChemComp-GOL / #3: Chemical | #4: Chemical | ChemComp-PO4 / | #5: Water | ChemComp-HOH / | |
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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: 2.27 Å3/Da / Density % sol: 45.45 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU-300R / Wavelength: 1.5418 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 28338 / % possible obs: 95.8 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Biso Wilson estimate: 33 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 19.1 |
-Processing
Software | Name: REFMAC / Version: 5.2.0005 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER / Resolution: 2.1→50 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.934 / SU B: 4.981 / SU ML: 0.133 / Cross valid method: THROUGHOUT / ESU R: 0.214 / ESU R Free: 0.187 / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.085 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refine LS restraints |
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