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- PDB-6wk1: SETD3 in Complex with an Actin Peptide with His73 Replaced with M... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6wk1 | ||||||
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Title | SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine | ||||||
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![]() | TRANSFERASE / TRANSFERASE-STRUCTURAL PROTEIN complex | ||||||
Function / homology | ![]() basal body patch / protein-histidine N-methyltransferase / peptidyl-histidine methylation / regulation of uterine smooth muscle contraction / protein-L-histidine N-tele-methyltransferase activity / actin modification / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton ...basal body patch / protein-histidine N-methyltransferase / peptidyl-histidine methylation / regulation of uterine smooth muscle contraction / protein-L-histidine N-tele-methyltransferase activity / actin modification / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / profilin binding / protein localization to bicellular tight junction / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / histone H3K36 methyltransferase activity / Adherens junctions interactions / regulation of stress fiber assembly / histone H3K4 methyltransferase activity / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / regulation of synaptic vesicle endocytosis / apical junction complex / regulation of focal adhesion assembly / positive regulation of wound healing / maintenance of blood-brain barrier / myofibril / sarcomere organization / positive regulation of muscle cell differentiation / NuA4 histone acetyltransferase complex / Recycling pathway of L1 / filamentous actin / calyx of Held / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / EPHB-mediated forward signaling / phagocytic vesicle / axonogenesis / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / FCGR3A-mediated phagocytosis / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / MAP2K and MAPK activation / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / PKMTs methylate histone lysines / platelet aggregation / VEGFA-VEGFR2 Pathway / cellular response to type II interferon / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / cell-cell junction / Clathrin-mediated endocytosis / actin binding / angiogenesis / RNA polymerase II-specific DNA-binding transcription factor binding / transcription coactivator activity / cytoskeleton / blood microparticle / hydrolase activity / positive regulation of cell migration / axon / focal adhesion / ubiquitin protein ligase binding / synapse / positive regulation of gene expression / chromatin / protein kinase binding / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dai, S. / Horton, J.R. / Cheng, X. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Characterization of SETD3 methyltransferase-mediated protein methionine methylation. Authors: Dai, S. / Holt, M.V. / Horton, J.R. / Woodcock, C.B. / Patel, A. / Zhang, X. / Young, N.L. / Wilkinson, A.W. / Cheng, X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 293.6 KB | Display | ![]() |
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PDB format | ![]() | 186.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 44.6 KB | Display | |
Data in CIF | ![]() | 64.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6wk2C ![]() 6mbjS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
-Protein/peptide / Protein , 2 types, 4 molecules YZAB
#1: Protein/peptide | Mass: 2861.296 Da / Num. of mol.: 2 / Mutation: H73M / Source method: obtained synthetically / Source: (synth.) ![]() #2: Protein | Mass: 67342.047 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q86TU7, protein-histidine N-methyltransferase |
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-Non-polymers , 5 types, 656 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/SAH.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/SAH.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-EDO / #5: Chemical | #6: Chemical | ChemComp-ACT / | #7: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.07 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 13, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.89→36 Å / Num. obs: 102262 / % possible obs: 93.6 % / Redundancy: 4.7 % / Biso Wilson estimate: 23.23 Å2 / CC1/2: 0.986 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 1.89→1.96 Å / Num. unique obs: 8146 / CC1/2: 0.526 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6MBJ Resolution: 1.89→36 Å / SU ML: 0.2308 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.1001 / Stereochemistry target values: GeoStd + Monomer Library
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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 mean: 28.19 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.89→36 Å
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Refine LS restraints |
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LS refinement shell |
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