PDBe 1mj9

X-ray diffraction
2.5Å resolution

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

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine. 
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo hexamer
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: MOZ/SAS family
Structure domains:

Ligands and Environments

2 bound ligands:

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