+Open data
-Basic information
Entry | Database: PDB / ID: 5ono | ||||||
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Title | Crystal Structure of Ectoine Synthase from P. lautus | ||||||
Components | L-ectoine synthase | ||||||
Keywords | METAL BINDING PROTEIN / Ectoine / synthase / osmolyte | ||||||
Function / homology | Function and homology information ectoine synthase / ectoine synthase activity / ectoine biosynthetic process / metal ion binding Similarity search - Function | ||||||
Biological species | Paenibacillus lautus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Bremer, E. | ||||||
Citation | Journal: Sci Rep / Year: 2019 Title: Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis. Authors: Czech, L. / Hoppner, A. / Kobus, S. / Seubert, A. / Riclea, R. / Dickschat, J.S. / Heider, J. / Smits, S.H.J. / Bremer, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ono.cif.gz | 65.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ono.ent.gz | 48.3 KB | Display | PDB format |
PDBx/mmJSON format | 5ono.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ono_validation.pdf.gz | 442.2 KB | Display | wwPDB validaton report |
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Full document | 5ono_full_validation.pdf.gz | 442.8 KB | Display | |
Data in XML | 5ono_validation.xml.gz | 8.1 KB | Display | |
Data in CIF | 5ono_validation.cif.gz | 10.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/on/5ono ftp://data.pdbj.org/pub/pdb/validation_reports/on/5ono | HTTPS FTP |
-Related structure data
Related structure data | 5onmC 5onnC 5bxxS 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: 15715.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Paenibacillus lautus (bacteria) / Gene: ectC, BK123_26285 / Production host: Escherichia coli (E. coli) References: UniProt: A0A1R1AV52, UniProt: A0A2A5LBI6*PLUS, ectoine synthase |
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#2: Chemical | ChemComp-FE / |
#3: Chemical | ChemComp-4CS / ( |
#4: 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: 3.22 Å3/Da / Density % sol: 61.86 % |
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Crystal grow | Temperature: 298 K / Method: batch mode / pH: 4.2 Details: 0.2 M ammonium sulfate, 0.1 M phosphate citrate pH 4.2, 20% (v/v) PEG 300, 10% (v/v) glycerol. PH range: 4.0-5.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.988 Å |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Oct 21, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.988 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→46.01 Å / Num. obs: 7282 / % possible obs: 99.3 % / Redundancy: 5.4 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 8.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5BXX Resolution: 2.5→46.007 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 3.22 / Phase error: 22.66
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→46.007 Å
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Refine LS restraints |
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LS refinement shell |
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