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human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)
Autogenerated by
for
adrian
Created on Wed, 2015-08-05 05:01, last updated on Wed, 2015-08-05 05:01
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General Information
This Model was autogenerated from the
"Quick Submit"
tool.
Model ID
3DPX-001738
Category
Proteins, Macromolecules and Viruses
Keyword(s)
Smyd proteins, MYND, SET domain, histone lysine methyltransferase, histone methylation, H3K4, TRANSFERASE
Protein Data Bank ID
3OXG
Experimental Method
X-RAY DIFFRACTION
Resolution
3.4
Model Details
Associated Species
Escherichia coli
Oligomeric Details
monomeric
R-Factor
0.2253
Scattering Type
x-ray
Attribution
PubMed ID
21 266 482
Digital Object Identifier (DOI)
10.1093/nar/gkr019
Citation Title
Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding.
Citation Year
2011
STL/VRML Files
PDB-3OXG-ribbon-secondary.wrl
PDB-3OXG-ribbon-rainbow.wrl
PDB-3OXG-ribbon-bychain.wrl
PDB-3OXG-ribbon.stl
PDB-3OXG-ribbon-thick.stl
PDB-3OXG-surf-hydropathy.wrl
PDB-3OXG-surf-coulombic.wrl
PDB-3OXG-surf-bychain.wrl
PDB-3OXG-surf.stl
PDB-3OXG.zip
X3D Files
PDB-3OXG-ribbon-secondary.x3d
PDB-3OXG-ribbon-rainbow.x3d
PDB-3OXG-ribbon-bychain.x3d
PDB-3OXG-ribbon.x3d
PDB-3OXG-ribbon-thick.x3d
PDB-3OXG-surf-hydropathy.x3d
PDB-3OXG-surf-coulombic.x3d
PDB-3OXG-surf-bychain.x3d
PDB-3OXG-surf.x3d
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