1xqh: Difference between revisions

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[[Image:1xqh.jpg|left|200px]]<br /><applet load="1xqh" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1xqh.jpg|left|200px]]
caption="1xqh, resolution 1.75&Aring;" />
 
'''Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH'''<br />
{{Structure
|PDB= 1xqh |SIZE=350|CAPTION= <scene name='initialview01'>1xqh</scene>, resolution 1.75&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43]
|GENE=
}}
 
'''Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1XQH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQH OCA].  
1XQH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQH OCA].  


==Reference==
==Reference==
Regulation of p53 activity through lysine methylation., Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D, Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15525938 15525938]
Regulation of p53 activity through lysine methylation., Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D, Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15525938 15525938]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: set9-p53 complex]]
[[Category: set9-p53 complex]]


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