› 2f5i

X-ray diffraction
2.3Å resolution

X-ray structure of spermidine/spermine N1-acetyltransferase (SAT) from Homo sapiens

Released:
DOI: 10.2210/pdb2f5i/pdb
PDB entry 2f5i coloured by chain, front view.
PDB entry 2f5i coloured by chain, side view.
PDB entry 2f5i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human spermidine/spermine N1-acetyltransferase (hSSAT): the first structure of a new sequence family of transferase homologous superfamily.
Zhu YQ, Zhu DY, Yin L, Zhang Y, Vonrhein C, Wang DC
Proteins 63 1127-31 (2006)
PMID: 16544326

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 179 amino acids
Theoretical weight: 21.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21673 (Residues: 1-171; Coverage: 100%)
Gene names: SAT, SAT1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43
Unit cell:
a: 46.336Å b: 46.336Å c: 180.489Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

3 mentions without citation

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