PDBe 5lkz

X-ray diffraction
2.5Å resolution

Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-coenzyme A.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 578 amino acids
Theoretical weight: 67.1 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: NEW Q09472 (Residues: 1043-1519, 1581-1666; Coverage: 20%)
Gene names: EP300, P300
Structure domains:

Ligands and Environments


Cofactor: Ligand COO 1 x COO
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2221
Unit cell:
a: 93.6Å b: 155.91Å c: 110.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.234
Expression system: Trichoplusia ni