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5ex3

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'''Unreleased structure'''
 
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The entry 5ex3 is ON HOLD until Paper Publication
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==Crystal structure of human SMYD3 in complex with a VEGFR1 peptide==
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<StructureSection load='5ex3' size='340' side='right' caption='[[5ex3]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
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Authors: Qiao, Q., Fu, W., Liu, N., Wang, M., Min, J., Zhu, B., Xu, R.M., Yang, N.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ex3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EX3 FirstGlance]. <br>
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Description: Crystal structure of human SMYD3 in complex with substrate
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
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[[Category: Wang, M]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ex0|5ex0]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ex3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ex3 OCA], [http://pdbe.org/5ex3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ex3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ex3 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Fu, W]]
[[Category: Liu, N]]
[[Category: Liu, N]]
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[[Category: Fu, W]]
 
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[[Category: Xu, R.M]]
 
[[Category: Min, J]]
[[Category: Min, J]]
[[Category: Qiao, Q]]
[[Category: Qiao, Q]]
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[[Category: Wang, M]]
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[[Category: Xu, R M]]
[[Category: Yang, N]]
[[Category: Yang, N]]
[[Category: Zhu, B]]
[[Category: Zhu, B]]
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[[Category: Cancer]]
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[[Category: Chromatin]]
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[[Category: Methylation]]
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[[Category: Set domain]]
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[[Category: Transferase]]

Revision as of 03:56, 10 March 2016

Crystal structure of human SMYD3 in complex with a VEGFR1 peptide

5ex3, resolution 2.41Å

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