3to7

X-ray diffraction
1.9Å resolution

Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine acetylated

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-170671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase ESA1 Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 33.15 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
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: I4132
Unit cell:
a: 183.04Å b: 183.04Å c: 183.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.226
Expression system: Escherichia coli