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Open data
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Basic information
Entry | Database: PDB / ID: 6agv | ||||||
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Title | Crystal structure of apo mouse MsrA | ||||||
![]() | Mitochondrial peptide methionine sulfoxide reductase | ||||||
![]() | OXIDOREDUCTASE / Methionine sulfoxide / MsrA | ||||||
Function / homology | ![]() Protein repair / L-methionine-(S)-S-oxide reductase activity / peptide-methionine (S)-S-oxide reductase / peptide-methionine (S)-S-oxide reductase activity / actin cytoskeleton / cellular response to oxidative stress / midbody / mitochondrion / nucleoplasm / plasma membrane ...Protein repair / L-methionine-(S)-S-oxide reductase activity / peptide-methionine (S)-S-oxide reductase / peptide-methionine (S)-S-oxide reductase activity / actin cytoskeleton / cellular response to oxidative stress / midbody / mitochondrion / nucleoplasm / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hwang, K.Y. / Kim, J.S. | ||||||
![]() | ![]() Title: Crystal structure of apo mouse MsrA Authors: Hwang, K.Y. / Kim, J.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 | ![]() | 72.4 KB | Display | ![]() |
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PDB format | ![]() | 42.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 535.9 KB | Display | ![]() |
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Full document | ![]() | 536.8 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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 on special symmetry positions |
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Components
#1: Protein | Mass: 26023.398 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9D6Y7, peptide-methionine (S)-S-oxide reductase |
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#2: Chemical | ChemComp-GOL / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.59 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.1M Tris pH 9.0, 0.2M NaCl, 26% polyethylene glycol 3350, 0.1M Sodium Iodide and were used in ratio of 1:1.35 (mouse MsrA and Trx peptide) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 15, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.62→50 Å / Num. obs: 165785 / % possible obs: 96.9 % / Redundancy: 5.3 % / Biso Wilson estimate: 16.2 Å2 / Rsym value: 0.037 / Net I/σ(I): 51.72 |
Reflection shell | Resolution: 1.62→1.65 Å / Mean I/σ(I) obs: 7.03 / Rsym value: 0.178 / % possible all: 91 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.46 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.62→30.68 Å
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Refine LS restraints |
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LS refinement shell |
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