4iao

X-ray diffraction
2.9Å resolution

Crystal structure of Sir2 C543S mutant in complex with SID domain of Sir4

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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-139136 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAD-dependent histone deacetylase SIR2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 492 amino acids
Theoretical weight: 55.68 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P06700 (Residues: 87-562; Coverage: 85%)
Gene names: D2714, MAR1, SIR2, YDL042C
Sequence domains:
Structure domains:
Regulatory protein SIR4 Chains: C, D
Molecule details ›
Chains: C, D
Length: 159 amino acids
Theoretical weight: 18.04 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P11978 (Residues: 737-893; Coverage: 12%)
Gene names: ASD1, SIR4, STE9, UTH2, YD9934.12, YDR227W
Sequence domains: Sir4 SID domain
Structure domains: Helix Hairpins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 166.406Å b: 178.752Å c: 121.564Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.227 0.269
Expression system: Escherichia coli