› 2b58

X-ray diffraction
1.95Å resolution

SSAT with coa_sp, spermine disordered, K26R mutant

Released:
DOI: 10.2210/pdb2b58/pdb
PDB entry 2b58 coloured by chain, front view.
PDB entry 2b58 coloured by chain, side view.
PDB entry 2b58 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target.
Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM
Proc Natl Acad Sci U S A 103 2063-8 (2006)
PMID: 16455797

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149349 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diamine acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 20.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21673 (Residues: 1-171; Coverage: 100%)
Gene names: SAT, SAT1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
No bound ligands
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P62
Unit cell:
a: 63.249Å b: 63.249Å c: 81.129Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.253
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases.
Casero et al. (2007)
4 more

4 mentions without citation

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