PDBe 4pzt

X-ray diffraction
2.8Å resolution

Crystal structure of p300 histone acetyltransferase domain in complex with an inhibitor, Acetonyl-Coenzyme A


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: 378 amino acids
Theoretical weight: 43.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q09472 (Residues: 1287-1664; Coverage: 16%)
Gene names: EP300, P300
Sequence domains: Histone acetylation protein

Ligands and Environments

Cofactor: Ligand SOP 1 x SOP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P43
Unit cell:
a: 63.681Å b: 63.681Å c: 104.122Å
α: 90° β: 90° γ: 90°
R R work R free
0.161 0.157 0.236
Expression system: Escherichia coli BL21(DE3)