› 2fck

X-ray diffraction
1.7Å resolution

Structure of a putative ribosomal-protein-serine acetyltransferase from Vibrio cholerae.

Released:
DOI: 10.2210/pdb2fck/pdb
PDB entry 2fck coloured by chain, front view.
PDB entry 2fck coloured by chain, side view.
PDB entry 2fck coloured by chain, top view.
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Primary publication:
Crystal structure of an acetyltransferase protein from Vibrio cholerae strain N16961.
Cuff ME, Li H, Moy S, Watson J, Cipriani A, Joachimiak A
Proteins 69 422-7 (2007)
PMID: 17623843

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 20.94 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3AIE8 (Residues: 1-178; Coverage: 100%)
Gene name: VC0395_A1479
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
Ligand NO3 12 x NO3
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 53.051Å b: 103.065Å c: 37.861Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.211 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.
Filippova et al. (2011)

3 mentions without citation

Protein frustratometer: a tool to localize energetic frustration in protein molecules.
Jenik et al. (2012)
2 more