› 2rim

X-ray diffraction
2.2Å resolution

Crystal structure of Rtt109

Released:
DOI: 10.2210/pdb2rim/pdb
PDB entry 2rim coloured by chain, front view.
PDB entry 2rim coloured by chain, side view.
PDB entry 2rim coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural insights into histone H3 lysine 56 acetylation by Rtt109.
Lin C, Yuan YA
Structure 16 1503-10 (2008)
PMID: 18707894

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-170501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase RTT109 Chain: A
Molecule details ›
Chain: A
Length: 457 amino acids
Theoretical weight: 52.75 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07794 (Residues: 1-436; Coverage: 100%)
Gene names: KAT11, KIM2, L1377, REM50, RTT109, YLL002W
Sequence domains: Histone acetylation protein

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2
Unit cell:
a: 147.401Å b: 69.233Å c: 55.661Å
α: 90° β: 94.93° γ: 90°
R-values:
R R work R free
0.219 0.216 0.259
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Signals and combinatorial functions of histone modifications.
Suganuma et al. (2011)
9 more

1 mention without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)