+Open data
-Basic information
Entry | Database: PDB / ID: 5zoa | ||||||
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Title | The crystal structure of a Thermobifida fusca cutinase | ||||||
Components | BTA-hydrolase 1 | ||||||
Keywords | HYDROLASE / cutin / Thermobifida fusca cutinase hydrolysis activity | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermobifida fusca (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.537 Å | ||||||
Authors | Dong, Q.L. / Wu, L. / Wu, J. / Zhou, J.H. | ||||||
Citation | Journal: To Be Published Title: The crystal structure of a cutinase from Thermobifida fusca Authors: Dong, Q.L. / Wu, L. / Wu, J. / Zhou, J.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5zoa.cif.gz | 119 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5zoa.ent.gz | 92 KB | Display | PDB format |
PDBx/mmJSON format | 5zoa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zo/5zoa ftp://data.pdbj.org/pub/pdb/validation_reports/zo/5zoa | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 28202.553 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermobifida fusca (bacteria) / Gene: bta1, cut_2 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: Q6A0I4, cutinase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.04 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 3.0M NaCl, 4.0%(v/v) Polypropylene glycel P400, 0.1M HEPES pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9796 Å |
Detector | Type: DECTRIS PILATUS 300K / Detector: PIXEL / Date: Jan 14, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.537→50 Å / Num. obs: 43283 / % possible obs: 99.8 % / Redundancy: 18.6 % / Net I/σ(I): 2 |
Reflection shell | Resolution: 1.54→1.6 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.537→28.542 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 16.68
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.537→28.542 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -15.074 Å / Origin y: 31.7331 Å / Origin z: 17.1818 Å
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Refinement TLS group | Selection details: all |