7wx6

X-ray diffraction
2.27Å resolution

A Legionella acetyltransferase VipF

Released:
Source organism: Legionella pneumophila
Primary publication:
Structural basis for the acetylation mechanism of the Legionella effector VipF.
Acta Crystallogr D Struct Biol 78 1110-1119 (2022)
PMID: 36048151

Function and Biology Details

Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-176902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 35.16 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5C8M4 (Residues: 1-286; Coverage: 100%)
Gene names: JBJ86_11720, vipF
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NFPSS BEAMLINE BL19U1
Spacegroup: C2221
Unit cell:
a: 72.047Å b: 84.525Å c: 105.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.253
Expression system: Escherichia coli