6oda: Difference between revisions

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<StructureSection load='6oda' size='340' side='right'caption='[[6oda]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
<StructureSection load='6oda' size='340' side='right'caption='[[6oda]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6oda]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ODA FirstGlance]. <br>
<table><tr><td colspan='2'>[[6oda]] is a 3 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=6ODA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ODA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C7:2-(4-CHLOROPHENYL)-4-[(3S)-PIPERIDIN-3-YLAMINO]THIENO[2,3-D]PYRIDAZINE-7-CARBOXAMIDE'>C7</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.88&#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_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C7:2-(4-CHLOROPHENYL)-4-[(3S)-PIPERIDIN-3-YLAMINO]THIENO[2,3-D]PYRIDAZINE-7-CARBOXAMIDE'>C7</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=6oda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oda OCA], [http://pdbe.org/6oda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oda RCSB], [http://www.ebi.ac.uk/pdbsum/6oda PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oda 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=6oda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oda OCA], [https://pdbe.org/6oda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oda RCSB], [https://www.ebi.ac.uk/pdbsum/6oda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oda ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>  
 
==See Also==
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone deacetylase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bair, K]]
[[Category: Bair K]]
[[Category: Barczak, N]]
[[Category: Barczak N]]
[[Category: Caravella, J]]
[[Category: Caravella J]]
[[Category: Conti, C]]
[[Category: Conti C]]
[[Category: Garcia-Dancey, R]]
[[Category: Garcia-Dancey R]]
[[Category: Han, B]]
[[Category: Han B]]
[[Category: Hardy, C]]
[[Category: Hardy C]]
[[Category: Lahdenranta, J]]
[[Category: Lahdenranta J]]
[[Category: Lancia, D]]
[[Category: Lancia Jr D]]
[[Category: Leng, C]]
[[Category: Leng C]]
[[Category: Li, P]]
[[Category: Li P]]
[[Category: Liu, C]]
[[Category: Liu C]]
[[Category: Martin, M]]
[[Category: Martin M]]
[[Category: Ng, P Y]]
[[Category: Ng PY]]
[[Category: Pardo, E]]
[[Category: Pardo E]]
[[Category: Rudnitskaya, A]]
[[Category: Rudnitskaya A]]
[[Category: Saldahna, A]]
[[Category: Saldahna A]]
[[Category: Tan, T]]
[[Category: Tan T]]
[[Category: Thomason, J J]]
[[Category: Thomason JJ]]
[[Category: Toms, A V]]
[[Category: Toms AV]]
[[Category: Yao, L]]
[[Category: Yao L]]
[[Category: Zablocki, M M]]
[[Category: Zablocki M-M]]
[[Category: Zhang, C]]
[[Category: Zhang C]]
[[Category: Zheng, X]]
[[Category: Zheng X]]
[[Category: Hdac8]]
[[Category: Hydrolase]]
[[Category: Hydroxamic acid]]

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