Brand  (β version)

PDB ID: 4BHW

Hetero Atom Contents

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain: Hide other chain(s)

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 PoSSuM
ZN Zinc ion PoSSuM

Structure summary

Code : 4BHW   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Structural basis for autoinhibition of the acetyltransferase activity of p300
Release Data : 2013-08-14
Compound :
mol_id molecule chains synonym
1 HISTONE ACETYLTRANSFERASE P300 A,B P300 HAT, E1A-ASSOCIATED PROTEIN P300
ec: 2.3.1.48
fragment: P300 CORE, RESIDUES 1043-1519,1581-1666
mutation: YES
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN TRICHOPLUSIA NI  (taxid:7111)
expression_system_common: CABBAGE LOOPER
expression_system_cell_line: High Five
expression_system_vector_type: BACULOVIRUS
Authors : Delvecchio, M., Gaucher, J., Aguilar-Gurrieri, C., Ortega, E., Panne, D.
Keywords : TRANSFERASE, BROMODOMAIN, PHD DOMAIN, RING DOMAIN, HAT DOMAIN, ENHANCEOSOME
Exp. method : X-RAY DIFFRACTION ( 2.799 Å )
Citation :

Structure of the P300 Catalytic Core and Implications for Chromatin Targeting and Hat Regulation

Delvecchio, M.,Gaucher, J.,Aguilar-Gurrieri, C.  et al.
(2013)  Nat.Struct.Mol.Biol.  20 : 1040

PubMed: 23934153
DOI: 10.1038/NSMB.2642

Reaction

Chain : A, B
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};