2h2f

X-ray diffraction
2.2Å resolution

The Structural basis for Sirtuin Substrate affinity

Released:
Primary publication:
The structural basis of sirtuin substrate affinity.
Biochemistry 45 7511-21 (2006)
PMID: 16768447

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-138128 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD-dependent protein deacetylase Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 27.57 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYW0 (Residues: 1-246; Coverage: 100%)
Gene names: TM_0490, cobB, sir2
Sequence domains: Sir2 family
Structure domains:
Cellular tumor antigen p53 Chain: B
Molecule details ›
Chain: B
Length: 18 amino acids
Theoretical weight: 2.1 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 372-389; Coverage: 5%)
Gene names: P53, TP53

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 45.645Å b: 59.31Å c: 105.953Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.246
Expression systems:
  • Escherichia coli
  • Not provided