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Yorodumi- PDB-5uun: Crystal structure of SARO_2595 from Novosphingobium aromaticivorans -
+Open data
-Basic information
Entry | Database: PDB / ID: 5uun | ||||||
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Title | Crystal structure of SARO_2595 from Novosphingobium aromaticivorans | ||||||
Components | Glutathione S-transferase-like protein | ||||||
Keywords | TRANSFERASE / Bioenergy / GLBRC / lignin valorization | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Novosphingobium aromaticivorans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å | ||||||
Authors | Bingman, C.A. / Kontur, W.S. / Olmsted, C.N. / Fox, B.G. / Donohue, T.J. | ||||||
Citation | Journal: J. Biol. Chem. / Year: 2018 Title: Novosphingobium aromaticivoransuses a Nu-class glutathioneS-transferase as a glutathione lyase in breaking the beta-aryl ether bond of lignin. Authors: Kontur, W.S. / Bingman, C.A. / Olmsted, C.N. / Wassarman, D.R. / Ulbrich, A. / Gall, D.L. / Smith, R.W. / Yusko, L.M. / Fox, B.G. / Noguera, D.R. / Coon, J.J. / Donohue, T.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5uun.cif.gz | 373.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5uun.ent.gz | 313.7 KB | Display | PDB format |
PDBx/mmJSON format | 5uun.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5uun_validation.pdf.gz | 2.3 MB | Display | wwPDB validaton report |
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Full document | 5uun_full_validation.pdf.gz | 2.4 MB | Display | |
Data in XML | 5uun_validation.xml.gz | 34.3 KB | Display | |
Data in CIF | 5uun_validation.cif.gz | 54.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uu/5uun ftp://data.pdbj.org/pub/pdb/validation_reports/uu/5uun | HTTPS FTP |
-Related structure data
Related structure data | 5uuoC 3c8eS 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: 32515.617 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199) (bacteria) Strain: ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199 Gene: Saro_2595 / Cell line (production host): B834 / Production host: Escherichia coli (E. coli) / References: UniProt: Q2G542 #2: Chemical | ChemComp-GSH / #3: Chemical | ChemComp-ACT / #4: 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: 3.1 Å3/Da / Density % sol: 60.38 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Saro protein at 277 mM was incubated with 10 mM reduced glutathione for 50 minutes prior to setting up crystallization experiments. An equal volume of protein solution and reservoir were ...Details: Saro protein at 277 mM was incubated with 10 mM reduced glutathione for 50 minutes prior to setting up crystallization experiments. An equal volume of protein solution and reservoir were deposited by a TTP Labtech Mosquito in a SD2 crystallization plate and allowed to equilibrate. The crystals were self-cryoprotected by the reservoir of 4 M ammonium acetate. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 30, 2016 |
Radiation | Monochromator: Silicon 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 1.45→43.97 Å / Num. obs: 140421 / % possible obs: 96.48 % / Redundancy: 13.2 % / Biso Wilson estimate: 13.23 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.04367 / Rpim(I) all: 0.01239 / Net I/σ(I): 36.36 |
Reflection shell | Resolution: 1.45→1.502 Å / Redundancy: 10.3 % / Rmerge(I) obs: 0.2047 / Mean I/σ(I) obs: 8.82 / Num. unique obs: 11067 / CC1/2: 0.986 / Rpim(I) all: 0.06599 / % possible all: 76.88 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3c8e chain A Resolution: 1.45→43.975 Å / SU ML: 0.08 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 11.39 / 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: 1.45→43.975 Å
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Refine LS restraints |
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LS refinement shell |
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