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5c89
From Proteopedia
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<StructureSection load='5c89' size='340' side='right'caption='[[5c89]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='5c89' size='340' side='right'caption='[[5c89]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5c89]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5c89]] 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=5C89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C89 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4YT:1-ETHYL-8-METHOXY-5-METHYL[1,2,4]TRIAZOLO[4,3-A]QUINOLINE'>4YT</scene></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=5c89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c89 OCA], [https://pdbe.org/5c89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c89 RCSB], [https://www.ebi.ac.uk/pdbsum/5c89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c89 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref> |
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Caflisch | + | [[Category: Caflisch A]] |
| - | [[Category: Wiedmer | + | [[Category: Wiedmer L]] |
| - | [[Category: Zhu | + | [[Category: Zhu J]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the human BRPF1 bromodomain in complex with 917
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