› 3bj8

X-ray diffraction
2.3Å resolution

Spermine/spermidine N1-acetyltransferase from mouse: Crystal structure of a ternary complex reveals solvent-mediated spermine binding

Released:
DOI: 10.2210/pdb3bj8/pdb
PDB entry 3bj8 coloured by chain, front view.
PDB entry 3bj8 coloured by chain, side view.
PDB entry 3bj8 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis.
Montemayor EJ, Hoffman DW
Biochemistry 47 9145-53 (2008)
PMID: 18690703

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155692 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diamine acetyltransferase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 171 amino acids
Theoretical weight: 20.04 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P48026 (Residues: 1-171; Coverage: 100%)
Gene names: Sat, Sat1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 4 x COA
1 bound ligand:
Ligand SPM 1 x SPM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 77.25Å b: 97.12Å c: 105.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.289
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Polyamine catabolism and disease.
Casero et al. (2009)
10 other articles

3 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
2 more