PDBe 3glr

X-ray diffraction
1.8Å resolution

Crystal Structure of human SIRT3 with acetyl-lysine AceCS2 peptide

Released:

Function and Biology Details

Reaction catalysed:
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD-dependent protein deacetylase sirtuin-3, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 31.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NTG7 (Residues: 118-399; Coverage: 71%)
Gene names: SIR2L3, SIRT3
Sequence domains: Sir2 family
Structure domains:
Acetyl-coenzyme A synthetase 2-like, mitochondrial Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.52 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9NUB1 (Residues: 638-649; Coverage: 2%)
Gene names: ACAS2L, ACSS1, KIAA1846

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2221
Unit cell:
a: 78.19Å b: 129.063Å c: 77.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.226
Expression systems:
  • Escherichia coli
  • Not provided