4mo2

X-ray diffraction
2Å resolution

Crystal Structure of UDP-N-acetylgalactopyranose mutase from Campylobacter jejuni

Released:

Function and Biology Details

Reaction catalysed:
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-171014 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-galactopyranose mutase C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 43.5 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0P8H5 (Residues: 1-368; Coverage: 100%)
Gene names: Cj1439c, glf
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand FDA 1 x FDA

Cofactor: Ligand FAD 1 x FAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 48.42Å b: 116.15Å c: 165.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.212
Expression system: Escherichia coli