5cnp

X-ray diffraction
2.38Å resolution

X-ray crystal structure of Spermidine n1-acetyltransferase from Vibrio cholerae.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-191926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spermidine N(1)-acetyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 176 amino acids
Theoretical weight: 21.12 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KL03 (Residues: 1-173; Coverage: 100%)
Gene names: VC_A0947, speG
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 159.931Å b: 134.176Å c: 77.477Å
α: 90° β: 114.43° γ: 90°
R-values:
R R work R free
0.188 0.185 0.236
Expression system: Escherichia coli BL21(DE3)