› 3biy

X-ray diffraction
1.7Å resolution

Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA

Released:
DOI: 10.2210/pdb3biy/pdb
PDB entry 3biy coloured by chain, front view.
PDB entry 3biy coloured by chain, side view.
PDB entry 3biy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis of protein acetylation by the p300/CBP transcriptional coactivator.
Liu X, Wang L, Zhao K, Thompson PR, Hwang Y, Marmorstein R, Cole PA
Nature 451 846-50 (2008)
PMID: 18273021

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 43.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q09472 (Residues: 1287-1666; Coverage: 16%)
Gene names: EP300, P300
Sequence domains: Histone acetylation protein

Ligands and Environments


Cofactor: Ligand 01K 1 x 01K
1 bound ligand:
Ligand BR 5 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A, null
Spacegroup: P43
Unit cell:
a: 61.513Å b: 61.513Å c: 101.153Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.213
Expression system: Escherichia coli

Quick links

Citations

66 review citations

Epigenetic protein families: a new frontier for drug discovery.
Arrowsmith et al. (2012)
65 more

49 mentions without citation

Protein lysine acetylation by p300/CBP.
Dancy et al. (2015)
48 more