› 4rmg

X-ray diffraction
1.88Å resolution

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
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-184915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacetylase sirtuin-2 Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 34.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IXJ6 (Residues: 56-356; Coverage: 77%)
Gene names: SIR2L, SIR2L2, SIRT2
Sequence domains: Sir2 family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand 3TE 1 x 3TE
Ligand NAD 1 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Unit cell:
a: 83.701Å b: 54.514Å c: 96.693Å
α: 90° β: 114.82° γ: 90°
R-values:
R R work R free
0.205 0.202 0.247
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Sirtuin activators and inhibitors: Promises, achievements, and challenges.
Dai et al. (2018)
26 more

25 mentions without citation

Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio.
Anderson et al. (2017)
24 more