› 1qsr

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A

Released:
DOI: 10.2210/pdb1qsr/pdb
PDB entry 1qsr coloured by chain, front view.
PDB entry 1qsr coloured by chain, side view.
PDB entry 1qsr coloured by chain, top view.
Source organism: Tetrahymena thermophila
Primary publication:
Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide.
Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R
Nature 401 93-8 (1999)
PMID: 10485713

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase GCN5 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

Quick links

Citations

38 review citations

Histone acetyltransferases.
Roth et al. (2001)
37 more

3 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
2 more