› 4rmi

X-ray diffraction
1.45Å 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

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165162 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
Ac-Lys-OTC peptide Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 475 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand 3TK 1 x 3TK
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 36.212Å b: 73.745Å c: 55.858Å
α: 90° β: 94.71° γ: 90°
R-values:
R R work R free
0.261 0.26 0.282
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

31 review citations

Sirtuin functions and modulation: from chemistry to the clinic.
Carafa et al. (2016)
30 more

6 mentions without citation

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.
Rumpf et al. (2015)
5 more