› 1m2h

X-ray diffraction
1.8Å resolution

Sir2 homologue S24A mutant-ADP ribose complex

Released:
DOI: 10.2210/pdb1m2h/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1m2h coloured by chain, front view.
PDB entry 1m2h coloured by chain, side view.
PDB entry 1m2h coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Structural basis for the NAD-dependent deacetylase mechanism of Sir2.
Chang JH, Kim HC, Hwang KY, Lee JW, Jackson SP, Bell SD, Cho Y
J Biol Chem 277 34489-98 (2002)
PMID: 12091395

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacylase 1 Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.64 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28597 (Residues: 1-245; Coverage: 100%)
Gene names: AF_1676, cobB1
Sequence domains: Sir2 family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand APR 1 x APR
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P21
Unit cell:
a: 35.707Å b: 85.299Å c: 44.853Å
α: 90° β: 112.08° γ: 90°
R-values:
R R work R free
0.187 0.187 0.215
Expression system: Escherichia coli

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Citations

24 review citations

The biochemistry of sirtuins.
Sauve et al. (2006)
23 more

1 mention without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)