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- PDB-5wt3: Pyrococcus abyssi methyltransferase PaTrm5a bound by MTA and cogn... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5wt3 | |||||||||
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Title | Pyrococcus abyssi methyltransferase PaTrm5a bound by MTA and cognate tRNA | |||||||||
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![]() | TRANSFERASE/RNA / methyltransferase / Trm5a / wyosine hypermodification / TRANSFERASE-RNA complex | |||||||||
Function / homology | ![]() tRNA N1-guanine methylation / tRNA (guanine37-N1)-methyltransferase / tRNA (guanine(37)-N1)-methyltransferase activity / tRNA methylation / Transferases; Transferring one-carbon groups; Methyltransferases / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Xie, W. / Wang, C. / Jia, Q. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insight into the methyltransfer mechanism of the bifunctional Trm5. Authors: Wang, C. / Jia, Q. / Zeng, J. / Chen, R. / Xie, W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 119.1 KB | Display | ![]() |
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PDB format | ![]() | 83.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 699.8 KB | Display | ![]() |
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Full document | ![]() | 704.7 KB | Display | |
Data in XML | ![]() | 16.7 KB | Display | |
Data in CIF | ![]() | 22.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5wt1C ![]() 2zznS C: citing same article ( S: Starting model for refinement |
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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: 38545.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: GE5 / Orsay / Gene: trm5a, PYRAB01130, PAB2272 / Production host: ![]() ![]() References: UniProt: Q9V2G1, tRNA (guanine37-N1)-methyltransferase |
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#2: RNA chain | Mass: 24551.658 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
#3: Chemical | ChemComp-MTA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.18 Å3/Da / Density % sol: 61.27 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: 45% MPD, 100 mM MES (pH 6.5), 200 mM NH4OAc |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: CCD / Date: Jun 6, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→50 Å / Num. obs: 13684 / % possible obs: 99.6 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 18.9 |
Reflection shell | Resolution: 3.2→3.31 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.174 / Mean I/σ(I) obs: 8.5 / CC1/2: 0.995 / % possible all: 98 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2ZZN Resolution: 3.204→49.14 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 31.1 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.204→49.14 Å
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Refine LS restraints |
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LS refinement shell |
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