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Open data
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Basic information
Entry | Database: PDB / ID: 1dmr | ||||||
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Title | OXIDIZED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS | ||||||
![]() | DMSO REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / REDUCTASE / DMSO / MOLYBDOPTERIN | ||||||
Function / homology | ![]() trimethylamine-N-oxide reductase activity / respiratory dimethylsulfoxide reductase / trimethylamine-N-oxide reductase / trimethylamine-N-oxide reductase (cytochrome c) activity / molybdenum ion binding / molybdopterin cofactor binding / anaerobic respiration / outer membrane-bounded periplasmic space / electron transfer activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mcalpine, A.S. / Bailey, S. | ||||||
![]() | Journal: J.Biol.Inorg.Chem. / Year: 1997 Title: Molybdenum Active Centre of Dmso Reductase from Rhodobacter Capsulatus: Crystal Structure of the Oxidised Enzyme at 1.82-A Resolution and the Dithionite-Reduced Enzyme at 2.8-A Resolution Authors: Mcalpine, A.S. / Mcewan, A.G. / Shaw, A. / Bailey, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 179.5 KB | Display | ![]() |
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PDB format | ![]() | 136.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 89524.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-6MO / | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 34.4 % Description: MODEL WAS FITTED TO THE PARTIAL MODEL FROM ISOMORPHOUS REPLACEMENT | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: 0.1M CITRATE BUFFER, PH 4.8 - 5.2 20 - 23% PEG 4000 20% ETHANOL, pH 5.5 PH range: 4.8-5.2 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion / PH range low: 5.5 / PH range high: 4.7 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 17, 1996 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 1.82→16.51 Å / Num. obs: 66800 / % possible obs: 97.4 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.82→1.94 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.269 / Mean I/σ(I) obs: 2.8 / % possible all: 91 |
Reflection | *PLUS Num. measured all: 283133 |
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Processing
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Refinement | Method to determine structure: ISOMORPHOUS REPLACEMENT, ![]() Starting model: DMSO REDUCTASE FROM RHODOBACTER SPHAEROIDES Resolution: 1.82→20 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.82→20 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.148 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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