PDBe 3biy

X-ray diffraction
1.7Å resolution

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


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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • 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:

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 R work R free
0.183 0.182 0.213
Expression system: Escherichia coli