› 5lkx

X-ray diffraction
2.52Å resolution

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

Released:
DOI: 10.2210/pdb5lkx/pdb
PDB entry 5lkx coloured by chain, front view.
PDB entry 5lkx coloured by chain, side view.
PDB entry 5lkx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of p300 in complex with acyl-CoA variants.
Kaczmarska Z, Ortega E, Goudarzi A, Huang H, Kim S, Márquez JA, Zhao Y, Khochbin S, Panne D
Nat Chem Biol 13 21-29 (2017)
PMID: 27820805

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: 578 amino acids
Theoretical weight: 67.1 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q09472 (Residues: 1043-1519, 1581-1666; Coverage: 23%)
Gene names: EP300, P300
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 1VU 1 x 1VU
3 bound ligands:
Ligand ZN 4 x ZN
Ligand DMS 1 x DMS
Ligand GOL 2 x GOL
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

Quick links

Citations

34 review citations

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
33 more

1 mention without citation

Structure of p300 in complex with acyl-CoA variants.
Kaczmarska et al. (2017)