5kch

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==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy into weak electron density==
==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy into weak electron density==
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<StructureSection load='5kch' size='340' side='right' caption='[[5kch]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='5kch' size='340' side='right'caption='[[5kch]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KCH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kch]] is a 1 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=5KCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KCH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6RN:4-(PYRIDIN-2-YLMETHYLAMINO)PHENOL'>6RN</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kco|5kco]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6RN:4-(PYRIDIN-2-YLMETHYLAMINO)PHENOL'>6RN</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETDB1, KIAA0067, KMT1E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kch OCA], [https://pdbe.org/5kch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kch RCSB], [https://www.ebi.ac.uk/pdbsum/5kch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kch ProSAT]</span></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=5kch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kch OCA], [http://pdbe.org/5kch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kch RCSB], [http://www.ebi.ac.uk/pdbsum/5kch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kch ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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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*[[Histone methyltransferase|Histone methyltransferase]]
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Brandao-Neto, J]]
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[[Category: Brandao-Neto J]]
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[[Category: Brown, P J]]
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[[Category: Brown PJ]]
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[[Category: Collins, P]]
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[[Category: Collins P]]
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[[Category: Delft, F von]]
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[[Category: Dobrovetsky E]]
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[[Category: Dobrovetsky, E]]
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[[Category: Douangamath A]]
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[[Category: Douangamath, A]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Harding RJ]]
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[[Category: Harding, R J]]
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[[Category: Mader P]]
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[[Category: Mader, P]]
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[[Category: Pearce N]]
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[[Category: Pearce, N]]
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[[Category: Santhakumar V]]
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[[Category: Structural genomic]]
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[[Category: Schapira M]]
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[[Category: Santhakumar, V]]
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[[Category: Tempel W]]
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[[Category: Schapira, M]]
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[[Category: Walker JR]]
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[[Category: Tempel, W]]
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[[Category: Von Delft F]]
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[[Category: Walker, J R]]
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[[Category: Diamond i04-1 xchem]]
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[[Category: Fragment screening]]
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[[Category: Pandda]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy into weak electron density

PDB ID 5kch

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