› 1mj9

X-ray diffraction
2.5Å resolution

Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A

Released:
DOI: 10.2210/pdb1mj9/pdb
PDB entry 1mj9 coloured by chain, front view.
PDB entry 1mj9 coloured by chain, side view.
PDB entry 1mj9 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: 33.36 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
1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: I4132
Unit cell:
a: 181.301Å b: 181.301Å c: 181.301Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.255
Expression system: Escherichia coli

Quick links

Citations

31 review citations

Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials.
Cheng et al. (2019)
30 more

4 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
3 more