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<StructureSection load='6bpi' size='340' side='right'caption='[[6bpi]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
<StructureSection load='6bpi' size='340' side='right'caption='[[6bpi]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6bpi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BPI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6BPI FirstGlance]. <br>
<table><tr><td colspan='2'>[[6bpi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BPI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=E2G:'>E2G</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E2G:~{N}-[[4-[2-(acetamidomethyl)phenyl]-5-methyl-1,2,4-triazol-3-yl]methyl]-2-azanyl-2-oxidanyl-ethanamide'>E2G</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6au2|6au2]], [[6au3|6au3]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bpi OCA], [https://pdbe.org/6bpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bpi RCSB], [https://www.ebi.ac.uk/pdbsum/6bpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bpi ProSAT]</span></td></tr>
<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://proteopedia.org/fgij/fg.htm?mol=6bpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bpi OCA], [http://pdbe.org/6bpi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bpi RCSB], [http://www.ebi.ac.uk/pdbsum/6bpi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bpi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>
[https://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: BROWN, P J]]
[[Category: BROWN PJ]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: CORLESS, V]]
[[Category: CORLESS V]]
[[Category: DIAZ, D B]]
[[Category: DELA SENA CC]]
[[Category: DOBROVETSKY, E]]
[[Category: DIAZ DB]]
[[Category: DONG, A]]
[[Category: DOBROVETSKY E]]
[[Category: Edwards, A M]]
[[Category: DONG A]]
[[Category: FRYE, S]]
[[Category: Edwards AM]]
[[Category: IQBAL, A]]
[[Category: FRYE S]]
[[Category: KENNEDY, S]]
[[Category: IQBAL A]]
[[Category: LIEW, S K]]
[[Category: KENNEDY S]]
[[Category: MADER, P]]
[[Category: LIEW SK]]
[[Category: Mendoza-Sanchez, R]]
[[Category: MADER P]]
[[Category: SCHAPIRA, M]]
[[Category: Mendoza-Sanchez R]]
[[Category: SENA, C C.DELA]]
[[Category: SCHAPIRA M]]
[[Category: Structural genomic]]
[[Category: SMIL D]]
[[Category: SMIL, D]]
[[Category: Santhakumar V]]
[[Category: Santhakumar, V]]
[[Category: TEMPEL W]]
[[Category: TEMPEL, W]]
[[Category: VEDADI M]]
[[Category: VEDADI, M]]
[[Category: YUDIN AK]]
[[Category: YUDIN, A K]]
[[Category: Epigenetic]]
[[Category: Fragment hit]]
[[Category: Methyl lysine reader]]
[[Category: Setdb1 tudor]]
[[Category: Sgc]]
[[Category: Transferase]]

Latest revision as of 09:44, 2 April 2025

Crystal structure of SETDB1 Tudor domain with aryl triazole fragment peptide conjugates

6bpi, resolution 1.64Å

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