1ma3

X-ray diffraction
2Å resolution

Structure of a Sir2 enzyme bound to an acetylated p53 peptide

Released:

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-128213 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD-dependent protein deacylase 2 Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 28.54 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O30124 (Residues: 1-253; Coverage: 100%)
Gene names: AF_0112, Sir2Af2, cobB2
Sequence domains: Sir2 family
Structure domains:
Cellular tumor antigen p53 Chain: B
Molecule details ›
Chain: B
Length: 18 amino acids
Theoretical weight: 2.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 372-389; Coverage: 5%)
Gene names: P53, TP53

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 34.892Å b: 35.591Å c: 184.683Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.254
Expression systems:
  • Escherichia coli
  • Not provided