1m2h

X-ray diffraction
1.8Å resolution

Sir2 homologue S24A mutant-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
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-128042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacylase 1 Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.64 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: PAL/PLS BEAMLINE 6B
Spacegroup: P21
Unit cell:
a: 35.707Å b: 85.299Å c: 44.853Å
α: 90° β: 112.08° γ: 90°
R-values:
R R work R free
0.187 0.187 0.215
Expression system: Escherichia coli