1qsr

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
histone acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 19.34 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27198 (Residues: 49-209; Coverage: 39%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 64.38Å b: 64.38Å c: 97.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.236 0.261
Expression system: Escherichia coli