› 1mja

X-ray diffraction
2.26Å resolution

Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A

Released:
DOI: 10.2210/pdb1mja/pdb
PDB entry 1mja coloured by chain, front view.
PDB entry 1mja coloured by chain, side view.
PDB entry 1mja coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
Yan Y, Harper S, Speicher DW, Marmorstein R
Nat Struct Biol 9 862-9 (2002)
PMID: 12368900

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 domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-170671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase ESA1 Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 33.41 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08649 (Residues: 160-435; Coverage: 62%)
Gene names: ESA1, O5257, YOR244W
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 1 x COA
No bound ligands
1 modified residue:
Ligand SCY 1 x SCY

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I4132
Unit cell:
a: 181.274Å b: 181.274Å c: 181.274Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.224
Expression system: Escherichia coli

Quick links

Citations

30 review citations

The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases.
Yang XJ. (2004)
29 more

6 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
5 more