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- PDB-1yx3: NMR structure of Allochromatium vinosum DsrC: Northeast Structura... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yx3 | ||||||
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Title | NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4 | ||||||
![]() | hypothetical protein DsrC | ||||||
![]() | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / DsrC / Dissimilatory sulfite reductase / gamma subunit / DsvC / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | ![]() Transferases; Transferring sulfur-containing groups; Sulfurtransferases / transferase activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Cort, J.R. / Dahl, C. / Montelione, G.T. / Kennedy, M.A. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Allochromatium vinosum DsrC: solution-state NMR structure, redox properties, and interaction with DsrEFH, a protein essential for purple sulfur bacterial sulfur oxidation. Authors: Cort, J.R. / Selan, U. / Schulte, A. / Grimm, F. / Kennedy, M.A. / Dahl, C. #1: Journal: J.Bacteriol. / Year: 2005 Title: Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum. Authors: Dahl, C. / Engels, S. / Pott-Sperling, A.S. / Schulte, A. / Sander, J. / Lubbe, Y. / Deuster, O. / Brune, D.C. #2: Journal: MICROBIOLOGY / Year: 1998 Title: Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Authors: Pott, A.S. / Dahl, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 688.3 KB | Display | ![]() |
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PDB format | ![]() | 573.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 345.9 KB | Display | ![]() |
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Full document | ![]() | 467.7 KB | Display | |
Data in XML | ![]() | 31.9 KB | Display | |
Data in CIF | ![]() | 55 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 14791.669 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 500 mM NaCl / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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NMR representative | Selection criteria: low energy, few violations, close to average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: low energy structures with fewest restraint violations Conformers calculated total number: 25 / Conformers submitted total number: 20 |