PDBe 4ig9

X-ray diffraction
2.64Å resolution

Structure of NAD-dependent protein deacetylase sirtuin-1 (open state, 2.64 A)

Released:
Source organism: Homo sapiens
Primary publication:
Structural and Functional Analysis of Human SIRT1.
J. Mol. Biol. (2013)
PMID: 24120939

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SirtT1 75 kDa fragment Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 281 amino acids
Theoretical weight: 31.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96EB6 (Residues: 234-510; Coverage: 37%)
Gene names: SIR2L1, SIRT1
Sequence domains: Sir2 family
Structure domains:
NAD-dependent protein deacetylase sirtuin-1 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 31 amino acids
Theoretical weight: 3.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96EB6 (Residues: 641-665; Coverage: 3%)
Gene names: SIR2L1, SIRT1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P43212
Unit cell:
a: 115.781Å b: 115.781Å c: 350.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.227 0.263
Expression system: Escherichia coli