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5va6

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==CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26==
==CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26==
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<StructureSection load='5va6' size='340' side='right' caption='[[5va6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5va6' size='340' side='right'caption='[[5va6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5va6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VA6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5va6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VA6 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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NMM:(2S)-2-AMINO-5-[(N-METHYLCARBAMIMIDOYL)AMINO]PENTANOIC+ACID'>NMM</scene></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=NMM:(2S)-2-AMINO-5-[(N-METHYLCARBAMIMIDOYL)AMINO]PENTANOIC+ACID'>NMM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5va6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5va6 OCA], [https://pdbe.org/5va6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5va6 RCSB], [https://www.ebi.ac.uk/pdbsum/5va6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5va6 ProSAT]</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=5va6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5va6 OCA], [http://pdbe.org/5va6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5va6 RCSB], [http://www.ebi.ac.uk/pdbsum/5va6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5va6 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ATXR5_RICCO ATXR5_RICCO]] Histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher activity on nucleosomes containing H3.1 than H3.3. Involved in the formation of constitutive heterochromatin and the silencing of heterochromatic elements (By similarity).
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[https://www.uniprot.org/uniprot/ATXR5_RICCO ATXR5_RICCO] Histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher activity on nucleosomes containing H3.1 than H3.3. Involved in the formation of constitutive heterochromatin and the silencing of heterochromatic elements (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__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: Bergamin, E]]
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[[Category: Large Structures]]
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[[Category: Blais, A]]
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[[Category: Ricinus communis]]
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[[Category: Brunzelle, J S]]
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[[Category: Bergamin E]]
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[[Category: Couture, J F]]
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[[Category: Blais A]]
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[[Category: Eram, M]]
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[[Category: Brunzelle JS]]
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[[Category: Joshi, M]]
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[[Category: Couture J-F]]
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[[Category: Malette, J]]
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[[Category: Eram M]]
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[[Category: Michaels, S D]]
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[[Category: Joshi M]]
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[[Category: Mongeon, V]]
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[[Category: Malette J]]
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[[Category: Sarvan, S]]
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[[Category: Michaels SD]]
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[[Category: Vedadi, M]]
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[[Category: Mongeon V]]
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[[Category: Yeung, S]]
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[[Category: Sarvan S]]
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[[Category: Nucleosome]]
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[[Category: Vedadi M]]
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[[Category: Transferase-dna binding protein complex]]
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[[Category: Yeung S]]

Current revision

CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26

PDB ID 5va6

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