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1peg

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Current revision (09:42, 16 August 2023) (edit) (undo)
 
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<StructureSection load='1peg' size='340' side='right'caption='[[1peg]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
<StructureSection load='1peg' size='340' side='right'caption='[[1peg]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1peg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1peg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.59&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ml9|1ml9]]</div></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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peg OCA], [https://pdbe.org/1peg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1peg RCSB], [https://www.ebi.ac.uk/pdbsum/1peg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1peg 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=1peg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peg OCA], [https://pdbe.org/1peg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1peg RCSB], [https://www.ebi.ac.uk/pdbsum/1peg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1peg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DIM5_NEUCR DIM5_NEUCR]] Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.<ref>PMID:11713521</ref> <ref>PMID:12679815</ref> <ref>PMID:12372305</ref> <ref>PMID:12887903</ref>
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[https://www.uniprot.org/uniprot/DIM5_NEUCR DIM5_NEUCR] Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.<ref>PMID:11713521</ref> <ref>PMID:12679815</ref> <ref>PMID:12372305</ref> <ref>PMID:12887903</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chrysonilia crassa]]
 
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[[Category: Histone-lysine N-methyltransferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cheng, X]]
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[[Category: Neurospora crassa]]
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[[Category: Horton, J R]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Khan, S I]]
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[[Category: Cheng X]]
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[[Category: Selker, E U]]
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[[Category: Horton JR]]
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[[Category: Tamaru, H]]
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[[Category: Khan SI]]
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[[Category: Yang, Z]]
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[[Category: Selker EU]]
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[[Category: Zhang, X]]
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[[Category: Tamaru H]]
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[[Category: A hybrid beta sheet formed by dim-5 and h3 tail]]
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[[Category: Yang Z]]
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[[Category: A suv39-type histone-h3 lys-9 methyltransferase]]
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[[Category: Zhang X]]
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[[Category: Post-set zinc-binding site]]
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[[Category: Pre-set triangular zn3cys9 zinc cluster]]
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[[Category: Set domain protein forms a knot-like substructure]]
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[[Category: Ternary structure of dim-5]]
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[[Category: Transferase]]
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Current revision

Structural basis for the product specificity of histone lysine methyltransferases

PDB ID 1peg

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