1mjb

X-ray diffraction
2.5Å resolution

Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A

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
homo hexamer
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: 33.39 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 ACO 1 x ACO
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I4132
Unit cell:
a: 181.783Å b: 181.783Å c: 181.783Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.229 0.234
Expression system: Escherichia coli