1m2n

X-ray diffraction
2.6Å resolution

Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex

Released:
Source organism: Archaeoglobus fulgidus
Primary publication:
Structural basis for the NAD-dependent deacetylase mechanism of Sir2.
J. Biol. Chem. 277 34489-98 (2002)
PMID: 12091395

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 27.43 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28597 (Residues: 1-245; Coverage: 100%)
Gene names: AF_1676, cobB1
Sequence domains: Sir2 family
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 84.72Å b: 84.72Å c: 193.087Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.308
Expression system: Escherichia coli