PDBe 5lkx

X-ray diffraction
2.52Å resolution

Crystal structure of the p300 acetyltransferase catalytic core with propionyl-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 1VU 1 x 1VU
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2221
Unit cell:
a: 93.81Å b: 155.26Å c: 109.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.207 0.239
Expression system: Trichoplusia ni