User:Lauryn Padgett/Sandbox 1

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===Overall Secondary Structure===
===Overall Secondary Structure===
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The secondary structure is 10% <scene name='81/811086/Helices/2'>helices</scene> and 37% <scene name='81/811086/Beta_sheets/2'>beta sheets</scene>. The helical composition includes 3 <scene name='81/811086/Alpha_helices/3'>alpha helices</scene>, with two residing in the SET domain and one in the C-terminal domain. The alpha helices in the SET domain are two turns while the C-terminal helix is by far the largest with 4 turns. There are also 2 <scene name='81/811086/3-10_helices/3'>3-10 helices</scene> in the SET domain which are each one turn. There are 21 total beta strands which reside in the N-terminal domain and the SET domain. The beta strands are primarily anti-parallel and multiple antiparallel strands are connected by <scene name='81/811086/Type_i_beta_turns/1'>Type I</scene> and <scene name='81/811086/Type_ii_beta_turns/1'>Type II</scene> turns.
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The secondary structure is composed of 10% <scene name='81/811086/Helices/3'>helices</scene> and 37% <scene name='81/811086/Beta_sheets/3'>beta sheets</scene>. The helical composition includes 3 <scene name='81/811086/Alpha_helices/4'>alpha helices</scene>, with two residing in the SET domain and one in the C-terminal domain. The alpha helices in the SET domain are two turns while the C-terminal helix is by far the largest with 4 turns. There are also 2 <scene name='81/811086/3-10_helices/4'>3-10 helices</scene> in the SET domain which are each one turn. There are 21 total beta strands which reside in the N-terminal domain and the SET domain. The beta strands are primarily anti-parallel and multiple antiparallel strands are connected by <scene name='81/811086/Type_i_beta_turns/3'>Type I</scene> and
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===C-Domain===
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The <scene name='81/811091/C_terminal_domain/1'>C-terminal Domain</scene> of the protein is essential for the binding and stabilization of the cofactor. The
The <scene name='81/811091/C_terminal_domain/1'>C-terminal Domain</scene> of the protein is essential for the binding and stabilization of the cofactor. The
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<scene name='81/811086/Alpha_helices/3'>alpha helices</scene>
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<scene name='81/811086/Alpha_helices/4'>alpha helices</scene>
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<scene name='81/811086/3-10_helices/3'>3-10 helices</scene>
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<scene name='81/811086/3-10_helices/4'>3-10 helices</scene>
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<scene name='81/811086/Helices/2'>helices</scene>
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<scene name='81/811086/Helices/3'>helices</scene>
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<scene name='81/811086/Beta_sheets/2'>beta sheets</scene>
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<scene name='81/811086/Beta_sheets/3'>beta sheets</scene>
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<scene name='81/811086/Type_i_beta_turns/1'>Type I</scene>
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<scene name='81/811086/Type_i_beta_turns/3'>Type I</scene>
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<scene name='81/811086/Type_ii_beta_turns/1'>Type II</scene>
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<scene name='81/811086/Beta_hairpin/2'>beta hairpin</scene>
<scene name='81/811086/Beta_hairpin/2'>beta hairpin</scene>
===SET Domain===
===SET Domain===

Revision as of 20:12, 2 April 2019

Homo sapiens Histone Methyl Transferase SET7/9 (KMT)==

KMT 1o9s

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Lauryn Padgett

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