2j0a

X-ray diffraction
1.8Å resolution

Structure of the catalytic domain of mouse Manic Fringe

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-126704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 162.6Å b: 41.4Å c: 39.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.219
Expression system: Spodoptera frugiperda