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New page: ==Crystal Structure of the SET Domain of Human SUV420H1 In Complex With Inhibitor== <StructureSection load='5wbv' size='340' side='right' caption='5wbv, resolution 2.30...
 
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==Crystal Structure of the SET Domain of Human SUV420H1 In Complex With Inhibitor==
==Crystal Structure of the SET Domain of Human SUV420H1 In Complex With Inhibitor==
<StructureSection load='5wbv' size='340' side='right' caption='[[5wbv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5wbv' size='340' side='right'caption='[[5wbv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5wbv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WBV FirstGlance]. <br>
<table><tr><td colspan='2'>[[5wbv]] 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=5WBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WBV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9ZY:2-chloro-5-(4-methyl-6-oxo-3-phenylpyrano[2,3-c]pyrazol-1(6H)-yl)benzoic+acid'>9ZY</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9ZY:2-chloro-5-(4-methyl-6-oxo-3-phenylpyrano[2,3-c]pyrazol-1(6H)-yl)benzoic+acid'>9ZY</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5wbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wbv OCA], [http://pdbe.org/5wbv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wbv RCSB], [http://www.ebi.ac.uk/pdbsum/5wbv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wbv ProSAT]</span></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=5wbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wbv OCA], [https://pdbe.org/5wbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wbv RCSB], [https://www.ebi.ac.uk/pdbsum/5wbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wbv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KMT5B_HUMAN KMT5B_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3.<ref>PMID:23720823</ref>
[https://www.uniprot.org/uniprot/KMT5B_HUMAN KMT5B_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3.<ref>PMID:23720823</ref>  
 
==See Also==
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H]]
[[Category: Large Structures]]
[[Category: Bountra, C]]
[[Category: Arrowsmith CH]]
[[Category: Brown, P J]]
[[Category: Bountra C]]
[[Category: Edwards, A M]]
[[Category: Brown PJ]]
[[Category: Halabelian, L]]
[[Category: Edwards AM]]
[[Category: Structural genomic]]
[[Category: Halabelian L]]
[[Category: Tempel, W]]
[[Category: Tempel W]]
[[Category: Methyltransferase]]
[[Category: Protein-inhibitor complex]]
[[Category: Set domain]]
[[Category: Sgc]]
[[Category: Transferase]]
[[Category: Transferase-inhibitor complex]]

Latest revision as of 14:10, 4 October 2023

Crystal Structure of the SET Domain of Human SUV420H1 In Complex With Inhibitor

5wbv, resolution 2.30Å

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