› 3bfp

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N'-diacetylbacillosamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylbacillosamine N-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 21.04 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0P9D1 (Residues: 2-195; Coverage: 100%)
Gene names: Cj1123c, pglD
Sequence domains: PglD N-terminal domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D, NSLS BEAMLINE X8C
Spacegroup: P63
Unit cell:
a: 86.462Å b: 86.462Å c: 65.547Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.225
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Protein glycosylation in bacteria: sweeter than ever.
Nothaft et al. (2010)
5 more

1 mention without citation

Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.
Olivier et al. (2008)