X-ray diffraction
2.1Å resolution

Structure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganese

Source organism: Mus musculus
Primary publication:
Structural insights into the Notch-modifying glycosyltransferase Fringe.
Nat. Struct. Mol. Biol. 13 945-6 (2006)
PMID: 16964258

Function and Biology Details

Reaction catalysed:
UDP-N-acetyl-alpha-D-glucosamine + [protein with EGF-like domain]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine) = UDP + [protein]-3-O-(N-acteyl-beta-D-glucosamine-(1->3)-alpha-L-fucosyl)-(L-serine/L-threonine)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-1,3-N-acetylglucosaminyltransferase manic fringe Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.55 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
  • Canonical: O09008 (Residues: 45-321; Coverage: 86%)
Gene name: Mfng
Sequence domains: Fringe-like
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 161.76Å b: 40.97Å c: 38.37Å
α: 90° β: 90° γ: 90°
R R work R free
0.18 0.177 0.221
Expression system: Spodoptera frugiperda