4qa2: Difference between revisions

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 ==Crystal structure of I243N HDAC8 in complex with SAHA==
-<StructureSection load='4qa2' size='340' side='right' caption='[[4qa2]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+<StructureSection load='4qa2' size='340' side='right'caption='[[4qa2]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4qa2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QA2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4qa2]] 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=4QA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QA2 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SHH:OCTANEDIOIC+ACID+HYDROXYAMIDE+PHENYLAMIDE'>SHH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.377&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qa0|4qa0]], [[4qa1|4qa1]], [[4qa3|4qa3]], [[4qa4|4qa4]], [[4qa5|4qa5]], [[4qa6|4qa6]], [[4qa7|4qa7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SHH:OCTANEDIOIC+ACID+HYDROXYAMIDE+PHENYLAMIDE'>SHH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qa2 OCA], [https://pdbe.org/4qa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qa2 RCSB], [https://www.ebi.ac.uk/pdbsum/4qa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qa2 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qa2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qa2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qa2 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qa2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Histone deacetylase]]
+[[Category: Homo sapiens]]
-[[Category: Bowman, C B.]]
+[[Category: Large Structures]]
-[[Category: Christianson, D W.]]
+[[Category: Bowman CB]]
-[[Category: Christianson, K E.]]
+[[Category: Christianson DW]]
-[[Category: Deardorff, M A.]]
+[[Category: Christianson KE]]
-[[Category: Decroos, C.]]
+[[Category: Deardorff MA]]
-[[Category: Moser, J A.S.]]
+[[Category: Decroos C]]
-[[Category: Arginase/deacetylase fold]]
+[[Category: Moser J-AS]]
-[[Category: Cornelia de lange syndrome]]
-[[Category: Enzyme inhibitor complex]]
-[[Category: Histone deacetylase]]
-[[Category: Hydrolase]]
-[[Category: Metalloenzyme]]