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Yorodumi- PDB-1h75: Structural basis for the thioredoxin-like activity profile of the... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1h75 | |||||||||
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Title | Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli. | |||||||||
Components | GLUTAREDOXIN-LIKE PROTEIN NRDH | |||||||||
Keywords | ELECTRON TRANSPORT / NRDH / THIOREDOXIN / GLUTAREDOXIN / REDOX PROTEIN | |||||||||
Function / homology | Function and homology information positive regulation of oxidoreductase activity / protein-disulfide reductase activity / cell redox homeostasis / electron transfer activity Similarity search - Function | |||||||||
Biological species | ESCHERICHIA COLI (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.7 Å | |||||||||
Authors | Stehr, M. / Schneider, G. / Aslund, F. / Holmgren, A. / Lindqvist, Y. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Structural Basis for the Thioredoxin-Like Activity Profile of the Glutaredoxin-Like Nrdh-Redoxin from Escherichia Coli Authors: Stehr, M. / Schneider, G. / Aslund, F. / Holmgren, A. / Lindqvist, Y. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h75.cif.gz | 24.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h75.ent.gz | 18 KB | Display | PDB format |
PDBx/mmJSON format | 1h75.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1h75_validation.pdf.gz | 421.5 KB | Display | wwPDB validaton report |
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Full document | 1h75_full_validation.pdf.gz | 422.7 KB | Display | |
Data in XML | 1h75_validation.xml.gz | 6.3 KB | Display | |
Data in CIF | 1h75_validation.cif.gz | 7.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h7/1h75 ftp://data.pdbj.org/pub/pdb/validation_reports/h7/1h75 | HTTPS FTP |
-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: 9152.472 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q47414, UniProt: P0AC65*PLUS |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.41 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 9.1 / Details: pH 9.10 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 1.0292 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0292 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→25 Å / Num. obs: 8503 / % possible obs: 96.4 % / Redundancy: 13.4 % / Biso Wilson estimate: 19.4 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 17.5 |
Reflection | *PLUS Lowest resolution: 25 Å / Num. measured all: 113655 |
Reflection shell | *PLUS % possible obs: 88.7 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.7→25 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Bsol: 80.6 Å2 / ksol: 0.37 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.1 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→25 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.2 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |