We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
6uhd
From Proteopedia
(Difference between revisions)
m (Protected "6uhd" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human histone acetyltransferase 1 (HAT1) in complex with Isobutyryl-CoA and K12A mutant variant of histone peptide H4== | |
| - | + | <StructureSection load='6uhd' size='340' side='right'caption='[[6uhd]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6uhd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UHD FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CO6:ISOBUTYRYL-COENZYME+A'>CO6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr> |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr> |
| - | [[Category: Arrowsmith, C | + | <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=6uhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uhd OCA], [http://pdbe.org/6uhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uhd RCSB], [http://www.ebi.ac.uk/pdbsum/6uhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uhd ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HAT1_HUMAN HAT1_HUMAN]] Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.<ref>PMID:9427644</ref> <ref>PMID:11585814</ref> <ref>PMID:20953179</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone acetyltransferase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bountra, C]] | ||
[[Category: Dong, A]] | [[Category: Dong, A]] | ||
| + | [[Category: Edwards, A M]] | ||
[[Category: Halabelian, L]] | [[Category: Halabelian, L]] | ||
| + | [[Category: Loppnau, P]] | ||
| + | [[Category: Structural genomic]] | ||
[[Category: Zeng, H]] | [[Category: Zeng, H]] | ||
| - | [[Category: | + | [[Category: Hat1]] |
| - | [[Category: | + | [[Category: Histone acetyltransferase 1]] |
| - | [[Category: | + | [[Category: Isobutyryl-coa]] |
| + | [[Category: Sgc]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:06, 16 October 2019
Crystal structure of human histone acetyltransferase 1 (HAT1) in complex with Isobutyryl-CoA and K12A mutant variant of histone peptide H4
| |||||||||||
