Brand  (β version)

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
01K [(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3r,20r)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate
BR Bromide ion
Code : 3BIY   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA
Release Data : 2008-02-12
Compound :
mol_id molecule chains synonym
1 Histone acetyltransferase p300 A E1A-associated protein p300
ec: 2.3.1.48
fragment: acetyltransferase domain
mutation: K1637R, M1652G
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: EP300, P300
expression_system_strain: BL21(DE3)-CodonPlus
expression_system_vector_type: Plasmid
expression_system_plasmid: pTYB2
Authors : Liu, X., Wang, L., Zhao, K., Thompson, P.R., Hwang, Y., Marmorstein, R., Cole, P.A.
Keywords : p300 HAT, Bisubstrate inhibitor, protein-inhibitor complex, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.70 Å )
Citation :

The structural basis of protein acetylation by the p300/CBP transcriptional coactivator

Liu, X.,Wang, L.,Zhao, K.  et al.
(2008)  Nature  451 : 846 - 850

PubMed: 18273021
DOI: 10.1038/nature06546

Chain : A
UniProt : Q09472 (EP300_HUMAN)
Reaction : Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:8945521};
Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)- (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:25818647};
Reaction=butanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-butanoyl- L-lysyl-[protein]; Xref=Rhea:RHEA:53912, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13708, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:137955; Evidence={ECO:0000250|UniProtKB:B2RWS6};
Reaction=L-lysyl-[protein] + propanoyl-CoA = CoA + H(+) + N(6)- propanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54020, Rhea:RHEA- COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:138019; Evidence={ECO:0000269|PubMed:17267393};
Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:29775581}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; Evidence={ECO:0000269|PubMed:29775581};