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- PDB-5m58: Crystal structure of CouO, a C-methyltransferase from Streptomyce... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5m58 | ||||||
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Title | Crystal structure of CouO, a C-methyltransferase from Streptomyces rishiriensis | ||||||
![]() | C-methyltransferase CouO | ||||||
![]() | TRANSFERASE / C-methyltransferase / CouO / Friedel-Craft alkylation / SAM / transfrease | ||||||
Function / homology | Methyltransferase domain 25 / Methyltransferase domain / antibiotic biosynthetic process / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / methylation / S-adenosyl-L-methionine-dependent methyltransferase superfamily / S-ADENOSYL-L-HOMOCYSTEINE / C-methyltransferase CouO![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pavkov-Keller, T. / Gruber, K. | ||||||
![]() | ![]() Title: Crystal Structure and Catalytic Mechanism of CouO, a Versatile C-Methyltransferase from Streptomyces rishiriensis. Authors: Pavkov-Keller, T. / Steiner, K. / Faber, M. / Tengg, M. / Schwab, H. / Gruber-Khadjawi, M. / Gruber, K. #1: Journal: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Year: 2012 Title: Crystallization of the novel S-adenosyl-L-methionine-dependent C-methyltransferase CouO from Streptomyces rishiriensis and preliminary diffraction data analysis. Authors: Lyskowski, A. / Tengg, M. / Steinkellner, G. / Schwab, H. / Gruber-Khadjawi, M. / Gruber, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 110.4 KB | Display | ![]() |
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PDB format | ![]() | 84.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 982 KB | Display | ![]() |
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Full document | ![]() | 985.1 KB | Display | |
Data in XML | ![]() | 21.8 KB | Display | |
Data in CIF | ![]() | 31.5 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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Unit cell |
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Components
#1: Protein | Mass: 25680.061 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9F8T9, Transferases; Transferring one-carbon groups; Methyltransferases #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.65 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop Details: 2.3 mg/ml CouO 12.5%(w/v) PEG 1000, 12.5%(w/v) PEG 3350, 12.5%(v/v) MPD, 0.03 M of each halide (sodium fluoride, sodium bromide and sodium iodide), 0.1 M MES/imidazole pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 13, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0507 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→40.98 Å / Num. all: 87179 / Num. obs: 25206 / % possible obs: 97.9 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.05→2.16 Å / Redundancy: 3 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 2.5 / Num. measured obs: 10510 / Num. unique all: 3498 / % possible all: 94.2 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.234 Å2
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Refinement step | Cycle: 1 / Resolution: 2.05→40 Å
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Refine LS restraints |
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