5ame
From Proteopedia
(Difference between revisions)
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<StructureSection load='5ame' size='340' side='right' caption='[[5ame]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='5ame' size='340' side='right' caption='[[5ame]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5ame]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AME FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ame]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AME FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PW3:4-ACETYL-PIPERAZIN-2-ONE'>PW3</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PW3:4-ACETYL-PIPERAZIN-2-ONE'>PW3</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5amf|5amf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5amf|5amf]]</td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref> | [[http://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref> | ||
| - | |||
| - | ==See Also== | ||
| - | *[[Bromodomain-containing protein|Bromodomain-containing protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
Revision as of 20:26, 24 January 2018
Crystal structure of the bromodomain of human surface epitope engineered BRD1A in complex with 3D Consortium fragment 4-acetyl- piperazin-2-one (SGC - Diamond I04-1 fragment screening)
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Categories: Human | Arrowsmith, C H | Bountra, C | Bowkett, D | Bradley, A | Brandao-Neto, J | Brennan, P | Burgess-Brown, N | Collins, P | Cox, O | Delft, F von | Douangamath, A | Edwards, E | Fairhead, M | Krojer, T | Ng, J T | Pearce, N M | Strain-Damerell, C | Talon, R | Wright, N | Bromodomain | Diamond i04-1 | Epigenetic | Fragmentscreening | Histone-binding protein | Sgc | Structural genomic | Transcription
