6bpi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:44, 2 April 2025) (edit) (undo)
 
Line 3: Line 3:
<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==
Line 19: Line 17:
__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]]
+

Current revision

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

PDB ID 6bpi

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bpi"
Personal tools