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- PDB-7y9c: Crystal structure of METTL9 in complex with SLC39A5 peptide and SAH -
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Open data
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Basic information
Entry | Database: PDB / ID: 7y9c | ||||||
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Title | Crystal structure of METTL9 in complex with SLC39A5 peptide and SAH | ||||||
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![]() | TRANSFERASE / METTL9 / SLC39A5 / histidine methyltransferase | ||||||
Function / homology | ![]() protein-L-histidine N-pros-methyltransferase activity / Transferases; Transferring one-carbon groups; Methyltransferases / methylation / endoplasmic reticulum / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Xie, H. / Wang, X. / Xu, C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for METTL9-mediated N1-histidine methylation. Authors: Wang, X. / Xie, H. / Guo, Q. / Cao, D. / Ru, W. / Zhao, S. / Zhu, Z. / Zhang, J. / Pan, W. / Yao, X. / Xu, 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 | ![]() | 136.4 KB | Display | ![]() |
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PDB format | ![]() | 103.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 997.4 KB | Display | ![]() |
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Full document | ![]() | 1002.7 KB | Display | |
Data in XML | ![]() | 26.7 KB | Display | |
Data in CIF | ![]() | 38.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7yf2C ![]() 7yf3C ![]() 7yf4C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 31554.012 Da / Num. of mol.: 2 / Mutation: L95A,F96A,L99A,F103A,V107A,F111A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9H1A3, Transferases; Transferring one-carbon groups; Methyltransferases #2: Protein/peptide | Mass: 1375.390 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: synthetic construct (others) #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.46 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 0.1 M MES monohydrate pH6.5, 12 % w/v PEG 20000, 0.2 M sodium thiocyanate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 18, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→43.05 Å / Num. obs: 34530 / % possible obs: 99.6 % / Redundancy: 6.4 % / CC1/2: 0.998 / Net I/σ(I): 14.6 |
Reflection shell | Resolution: 2.1→2.16 Å / Num. unique obs: 34530 / CC1/2: 0.88 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: model from alphafold2 Resolution: 2.1→31.829 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.85 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 65.12 Å2 / Biso mean: 28.5783 Å2 / Biso min: 14.35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.1→31.829 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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