Brand  (β version)

PDB ID: 6GYR

Hetero Atom Contents

color scheme of protein:

hetatm:

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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 : 6GYR   PDBj   RCSB PDB   PDBe
Header : GENE REGULATION
Title : Transcription factor dimerization activates the p300 acetyltransferase
Release Data : 2018-10-17
Compound :
mol_id molecule chains synonym
1 Histone acetyltransferase p300 A,B,C,D p300 HAT,E1A-associated protein p300,Histone butyryltransferase p300,Histone crotonyltransferase p300,Protein propionyltransferase p300
ec: 2.3.1.48,2.3.1.-
mutation: Y1467F
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Trichoplusia  (taxid:7110)
gene: EP300, P300
Authors : Panne, D., Ortega, E.
Keywords : P300, CBP, acetyltransferase, Chromatin, transcriptional regulation, GENE REGULATION
Exp. method : X-RAY DIFFRACTION ( 3.1 Å )
Citation :

Transcription factor dimerization activates the p300 acetyltransferase.

Ortega, E.,Rengachari, S.,Ibrahim, Z.  et al.
(2018)  Nature  562 : 538 - 544

PubMed: 30323286
DOI: 10.1038/s41586-018-0621-1

Reaction

Chain : A, B, C, D
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};