5yjo: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5yjo is ~~ON HOLD~~ ~~until Paper Publication~~

==Crystal structure of SmyD3 in complex with covalent inhibitor 4==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5yjo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJO OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJO FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=8W0:propyl+(3~{S})-4-[[(6~{R})-6-(aminomethyl)-5,6,7,8-tetrahydroacridin-3-yl]carbonyl]-3-methyl-piperazine-1-carboxylate'>8W0</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjo OCA], [http://pdbe.org/5yjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yjo RCSB], [http://www.ebi.ac.uk/pdbsum/5yjo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjo ProSAT]</td></tr>

</table>

== Function ==

[[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>

== References ==

__TOC__

</StructureSection>

[[Category: Histone-lysine N-methyltransferase]]

[[Category: Baburajendran, N]]

[[Category: E, J Anna]]

[[Category: Covalent inhibitor]]

[[Category: Methyltransferase]]

[[Category: Methyltransferase inhibitor]]

[[Category: Transferase-inhibitor complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5yjo is ON HOLD  until Paper Publication
+==Crystal structure of SmyD3 in complex with covalent inhibitor 4==
+<StructureSection load='5yjo' size='340' side='right' caption='[[5yjo]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5yjo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJO FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8W0:propyl+(3~{S})-4-[[(6~{R})-6-(aminomethyl)-5,6,7,8-tetrahydroacridin-3-yl]carbonyl]-3-methyl-piperazine-1-carboxylate'>8W0</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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>
+<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=5yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjo OCA], [http://pdbe.org/5yjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yjo RCSB], [http://www.ebi.ac.uk/pdbsum/5yjo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjo ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Histone-lysine N-methyltransferase]]
+[[Category: Baburajendran, N]]
+[[Category: E, J Anna]]
+[[Category: Covalent inhibitor]]
+[[Category: Methyltransferase]]
+[[Category: Methyltransferase inhibitor]]
+[[Category: Transferase-inhibitor complex]]