› 5ojn

X-ray diffraction
1.8Å resolution

Sirtuin 4 from Xenopus tropicalis in complex with thioacetyl-ADP-ribose

Released:
DOI: 10.2210/pdb5ojn/pdb
PDB entry 5ojn coloured by chain, front view.
PDB entry 5ojn coloured by chain, side view.
PDB entry 5ojn coloured by chain, top view.
Source organism: Xenopus tropicalis
Primary publication:
Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features.
Pannek M, Simic Z, Fuszard M, Meleshin M, Rotili D, Mai A, Schutkowski M, Steegborn C
Nat Commun 8 1513 (2017)
PMID: 29138502

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-173324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacylase Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 32.1 KDa
Source organism: Xenopus tropicalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q28CB4 (Residues: 32-315; Coverage: 88%)
Gene names: TGas015j14.1-001, sir2l4, sirt4
Sequence domains: Sir2 family

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand 9X8 1 x 9X8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 68.97Å b: 74.88Å c: 109.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.155 0.209
Expression system: Escherichia coli

Quick links

Citations

23 review citations

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

1 mention without citation

Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features.
Pannek et al. (2017)