X-ray diffraction
2.3Å resolution

Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide


Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 19.46 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli BL21
  • Canonical: Q27198 (Residues: 48-209; Coverage: 39%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase
Histone H3 Chain: B
Molecule details ›
Chain: B
Length: 19 amino acids
Theoretical weight: 2.02 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
  • Canonical: P61830 (Residues: 6-24; Coverage: 14%)
Gene names: HHT1, HHT2, N2749, SIN2, YBR010W, YBR0201, YNL031C

Ligands and Environments

Cofactor: Ligand COA 1 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3221
Unit cell:
a: 64.73Å b: 64.73Å c: 96.416Å
α: 90° β: 90° γ: 120°
R R work R free
0.236 0.236 0.26
Expression systems:
  • Escherichia coli BL21
  • Not provided