Brand  (β version)

PDB ID: 3BIY

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show 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
BR Bromide ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

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

Reaction

Chain : A
UniProt : Q09472 (EP300_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+) 2.3.1.48 PubMed:14645221, PubMed:21131905, PubMed:23415232, PubMed:23934153, PubMed:25818647, PubMed:8945521
left-to-right
L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+) - PubMed:15448695, PubMed:15653507, PubMed:16285960, PubMed:17761950, PubMed:22084251, PubMed:24120661, PubMed:26990986, PubMed:30197302, PubMed:32561715
left-to-right PubMed:15653507, PubMed:16285960, PubMed:15448695, PubMed:30197302, PubMed:32561715
N(6)-methyl-L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-N(6)- methyl-L-lysyl-[histone] + CoA + H(+) - PubMed:37731000
left-to-right
(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L- lysyl-[protein] + CoA + H(+) - PubMed:25818647
-
butanoyl-CoA + L-lysyl-[protein] = N(6)-butanoyl-L-lysyl- [protein] + CoA + H(+) - UniProtKB:B2RWS6
-
propanoyl-CoA + L-lysyl-[protein] = N(6)-propanoyl-L-lysyl- [protein] + CoA + H(+) - PubMed:17267393
-
2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2- hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+) - PubMed:29775581
left-to-right
(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L- lysyl-[protein] + CoA + H(+) - PubMed:31645732
left-to-right