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Open data
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Basic information
Entry | Database: PDB / ID: 4qpn | ||||||
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Title | Crystal Structure of Human Methyltransferase-Like Protein 21B | ||||||
![]() | Protein-lysine methyltransferase METTL21B | ||||||
![]() | TRANSFERASE / structural genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() peptidyl-lysine methylation / intracellular anatomical structure / protein-lysine N-methyltransferase activity / heat shock protein binding / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / centrosome / protein-containing complex / nucleoplasm / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Tempel, W. / Hong, B.S. / Seitova, A. / He, H. / Li, Y. / Graslund, S. / Arrowsmith, C.H. / Edwards, A.M. / Brown, P.J. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Crystal Structure of Human Methyltransferase-Like Protein 21B Authors: Tempel, W. / Hong, B.S. / Seitova, A. / He, H. / Li, Y. / Graslund, S. / Arrowsmith, C.H. / Edwards, A.M. / Brown, P.J. / Structural Genomics Consortium (SGC) | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.8 KB | Display | ![]() |
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PDB format | ![]() | 81.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 699.1 KB | Display | ![]() |
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Full document | ![]() | 699 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 17.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4lecS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 24994.111 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q96AZ1, Transferases; Transferring one-carbon groups; Methyltransferases | ||||
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#2: Chemical | ChemComp-SAH / | ||||
#3: Chemical | #4: Chemical | ChemComp-UNX / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.67 Å3/Da / Density % sol: 26.53 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion Details: 20% PEG-3350, 0.2 M tri-lithium citrate. Protein sample was incubated with SAH overnight. Endopeptidase was added to the protein sample immediately prior to crystallization set up, vapor ...Details: 20% PEG-3350, 0.2 M tri-lithium citrate. Protein sample was incubated with SAH overnight. Endopeptidase was added to the protein sample immediately prior to crystallization set up, vapor diffusion, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: adsc q315 / Detector: CCD / Date: Jun 12, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→38.78 Å / Num. obs: 45170 / % possible obs: 100 % / Redundancy: 11.1 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 19.6 |
Reflection shell | Resolution: 1.25→1.27 Å / Redundancy: 10.8 % / Rmerge(I) obs: 0.956 / Mean I/σ(I) obs: 3 / Num. measured all: 23595 / Num. unique all: 2181 / % possible all: 100 |
-Phasing
Phasing | Method: ![]() |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: solved with data from isomorphous crystal. model based on pdb entry 4LEC. Resolution: 1.25→33.48 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.97 / WRfactor Rfree: 0.1619 / WRfactor Rwork: 0.1185 / Occupancy max: 1 / Occupancy min: 0.3 / FOM work R set: 0.9047 / SU B: 1.482 / SU ML: 0.029 / SU R Cruickshank DPI: 0.0424 / SU Rfree: 0.0449 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.042 / ESU R Free: 0.045 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: Structure was solved and model was automatically built (ARP/WARP) using data from a nearly isomorphous crystal. COOT was used for interactive model building. Model geometry was evaluated with MOLPROBITY.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 65.27 Å2 / Biso mean: 12.1595 Å2 / Biso min: 4.05 Å2
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Refinement step | Cycle: LAST / Resolution: 1.25→33.48 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.25→1.282 Å / Total num. of bins used: 20
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