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X-ray diffraction
1.7Å 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-168057 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD-dependent protein deacetylase sirtuin-2 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IXJ6 (Residues: 52-356; Coverage: 75%)
Gene names: SIR2L, SIR2L2, SIRT2
Sequence domains: Sir2 family
myristoyl thiourea inhibitor, No.23 Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 522 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand F4R 1 x F4R
1 modified residue:
Ligand AIB 1 x AIB

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 35.83Å b: 65.494Å c: 114.889Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.251 0.32
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

Epigenetic meets metabolism: novel vulnerabilities to fight cancer.
Scumaci et al. (2023)
6 other articles

1 mention without citation

Mechanism-based inhibitors of SIRT2: structure-activity relationship, X-ray structures, target engagement, regulation of α-tubulin acetylation and inhibition of breast cancer cell migration.
Nielsen et al. (2021)