› 4pzt

X-ray diffraction
2.8Å resolution

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

Released:
DOI: 10.2210/pdb4pzt/pdb
PDB entry 4pzt coloured by chain, front view.
PDB entry 4pzt coloured by chain, side view.
PDB entry 4pzt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the p300 histone acetyltransferase bound to acetyl-coenzyme A and its analogues.
Maksimoska J, Segura-Peña D, Cole PA, Marmorstein R
Biochemistry 53 3415-22 (2014)
PMID: 24819397

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: 378 amino acids
Theoretical weight: 43.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • 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:
Ligand DMS 3 x DMS
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-values:
R R work R free
0.161 0.157 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Exploitation of EP300 and CREBBP Lysine Acetyltransferases by Cancer.
Attar et al. (2017)
8 more

4 mentions without citation

Regulation of Thermogenic Adipocyte Differentiation and Adaptive Thermogenesis Through Histone Acetylation.
Ong et al. (2020)
3 more