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Yorodumi- PDB-1wgb: Crystal structure of a probable flavoprotein from Thermus thermop... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wgb | ||||||
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Title | Crystal structure of a probable flavoprotein from Thermus thermophilus HB8 | ||||||
Components | probable flavoprotein | ||||||
Keywords | OXIDOREDUCTASE / flavoprotein / HB8 / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor / monooxygenase activity / FMN binding Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2 Å | ||||||
Authors | Imagawa, T. / Tsuge, H. / Utsunomiya, H. / Yokoyama, S. / Kuramitsu, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Crystal structure of a probable flavoprotein from Thermus thermophilus HB8 Authors: Imagawa, T. / Tsuge, H. / Utsunomiya, H. / Yokoyama, S. / Kuramitsu, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wgb.cif.gz | 41.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wgb.ent.gz | 32.4 KB | Display | PDB format |
PDBx/mmJSON format | 1wgb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wgb_validation.pdf.gz | 418.7 KB | Display | wwPDB validaton report |
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Full document | 1wgb_full_validation.pdf.gz | 421.1 KB | Display | |
Data in XML | 1wgb_validation.xml.gz | 9.6 KB | Display | |
Data in CIF | 1wgb_validation.cif.gz | 13 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wg/1wgb ftp://data.pdbj.org/pub/pdb/validation_reports/wg/1wgb | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 17890.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: Q72LK7 |
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#2: 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: 2.29 Å3/Da / Density % sol: 46.22 % |
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-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B2 / Wavelength: 0.97923, 0.9000, 0.97954 | ||||||||||||
Radiation | Monochromator: Si 111 CHANNEL / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.9→34 Å / Num. all: 13607 / Num. obs: 13607 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.85 % / Rmerge(I) obs: 0.038 | ||||||||||||
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 9.09 % / Rmerge(I) obs: 0.049 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2→34 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→34 Å
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Refine LS restraints |
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