+Open data
-Basic information
Entry | Database: PDB / ID: 5iq0 | ||||||
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Title | Crystal structure of Esterase mutant - F72G | ||||||
Components | Esterase | ||||||
Keywords | HYDROLASE / Esterase / Est25 / Hormone-Sensitive Lipase | ||||||
Function / homology | short-chain carboxylesterase activity / Alpha/beta hydrolase fold-3 / alpha/beta hydrolase fold / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / Esterase Function and homology information | ||||||
Biological species | uncultured bacterium (environmental samples) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.799 Å | ||||||
Authors | Seok, S.-H. / Seo, M.-D. / Kim, J. / Ryu, Y. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of Esterase mutant - F72G Authors: Seok, S.-H. / Seo, M.-D. / Kim, J. / Ryu, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5iq0.cif.gz | 285.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5iq0.ent.gz | 231.1 KB | Display | PDB format |
PDBx/mmJSON format | 5iq0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5iq0_validation.pdf.gz | 461.6 KB | Display | wwPDB validaton report |
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Full document | 5iq0_full_validation.pdf.gz | 480.9 KB | Display | |
Data in XML | 5iq0_validation.xml.gz | 58.8 KB | Display | |
Data in CIF | 5iq0_validation.cif.gz | 86.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iq/5iq0 ftp://data.pdbj.org/pub/pdb/validation_reports/iq/5iq0 | HTTPS FTP |
-Related structure data
Related structure data | 5iq2C 5iq3C 1jkmS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 38248.785 Da / Num. of mol.: 4 / Mutation: F72G Source method: isolated from a genetically manipulated source Source: (gene. exp.) uncultured bacterium (environmental samples) Production host: Escherichia coli (E. coli) / References: UniProt: Q4TZQ3 #2: 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: 3.03 Å3/Da / Density % sol: 59.36 % |
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Crystal grow | Temperature: 299 K / Method: microbatch / pH: 7 / Details: 2.4 M sodium malonate (pH 7.0) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 0.97935 Å |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Mar 14, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97935 Å / Relative weight: 1 |
Reflection | Resolution: 1.799→36.17 Å / Num. obs: 167878 / % possible obs: 97.9 % / Redundancy: 5.6 % / Net I/σ(I): 44.86 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1JKM Resolution: 1.799→36.167 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 19.32 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.799→36.167 Å
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Refine LS restraints |
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LS refinement shell |
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