› 5mar

X-ray diffraction
1.89Å 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacetylase sirtuin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 34.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8IXJ6 (Residues: 56-356; Coverage: 77%)
Gene names: SIR2L, SIR2L2, SIRT2
Sequence domains: Sir2 family

Ligands and Environments

7 bound ligands:
Ligand ZN 2 x ZN
Ligand AR6 2 x AR6
Ligand 7KE 2 x 7KE
Ligand EDO 2 x EDO
Ligand DMS 9 x DMS
Ligand GOL 4 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 76.557Å b: 76.709Å c: 113.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.194
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

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

3 mentions without citation

Structural basis for the activation and inhibition of Sirtuin 6 by quercetin and its derivatives.
You et al. (2019)
2 more