1q17

X-ray diffraction
2.7Å resolution

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide

Released:

Function and Biology Details

Reaction catalysed:
(1a) [protein]-N(6)-acetyl-L-lysine + NAD(+) = [protein]-N(6)-(1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl)-L-lysine + nicotinamide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-156860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacetylase HST2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 300 amino acids
Theoretical weight: 33.81 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53686 (Residues: 1-294; Coverage: 82%)
Gene names: HST2, LPA2C, YPL015C
Sequence domains: Sir2 family
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 146.159Å b: 109.682Å c: 85.825Å
α: 90° β: 104.9° γ: 90°
R-values:
R R work R free
0.217 0.186 0.247
Expression system: Escherichia coli