› 1ygh

X-ray diffraction
1.9Å resolution

HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE

Released:
DOI: 10.2210/pdb1ygh/pdb
PDB entry 1ygh coloured by chain, front view.
PDB entry 1ygh coloured by chain, side view.
PDB entry 1ygh coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
Trievel RC, Rojas JR, Sterner DE, Venkataramani RN, Wang L, Zhou J, Allis CD, Berger SL, Marmorstein R
Proc Natl Acad Sci U S A 96 8931-6 (1999)
PMID: 10430873

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-169876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase GCN5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 19.25 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03330 (Residues: 99-262; Coverage: 37%)
Gene names: ADA4, GCN5, SWI9, YGR252W
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 40.04Å b: 66.51Å c: 80.19Å
α: 90° β: 97.71° γ: 90°
R-values:
R R work R free
0.195 0.195 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

31 review citations

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

8 mentions without citation

Catalysis and substrate selection by histone/protein lysine acetyltransferases.
Berndsen et al. (2008)
7 more