3s32

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==Crystal structure of Ash2L N-terminal domain==
==Crystal structure of Ash2L N-terminal domain==
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<StructureSection load='3s32' size='340' side='right' caption='[[3s32]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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<StructureSection load='3s32' size='340' side='right'caption='[[3s32]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s32]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S32 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s32]] 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=3S32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S32 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=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]] 2.45&#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=MSE:SELENOMETHIONINE'>MSE</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASH2L, ASH2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3s32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s32 OCA], [https://pdbe.org/3s32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s32 RCSB], [https://www.ebi.ac.uk/pdbsum/3s32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s32 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=3s32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s32 RCSB], [http://www.ebi.ac.uk/pdbsum/3s32 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>
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[https://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3s32" style="background-color:#fffaf0;"></div>
==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/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Avdic, V]]
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[[Category: Large Structures]]
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[[Category: Blais, A]]
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[[Category: Avdic V]]
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[[Category: Brand, M]]
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[[Category: Blais A]]
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[[Category: Brunzelle, J S]]
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[[Category: Brand M]]
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[[Category: Chaturvedi, C P]]
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[[Category: Brunzelle JS]]
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[[Category: Couture, J F]]
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[[Category: Chaturvedi C-P]]
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[[Category: Lanouette, S]]
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[[Category: Couture J-F]]
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[[Category: Sarvan, S]]
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[[Category: Lanouette S]]
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[[Category: Tremblay, V]]
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[[Category: Sarvan S]]
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[[Category: Zhang, P]]
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[[Category: Tremblay V]]
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[[Category: C4-zinc finger]]
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[[Category: Zhang P]]
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[[Category: Chromatin]]
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[[Category: Helix-wing-helix]]
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[[Category: Histone]]
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[[Category: Myeloid lymphoma leukemia protein]]
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[[Category: Nucleus]]
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[[Category: Transcription]]
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[[Category: Trithorax]]
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[[Category: Trithorax group protein]]
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Current revision

Crystal structure of Ash2L N-terminal domain

PDB ID 3s32

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