› 6bji

X-ray diffraction
1.54Å resolution

Function and Biology Details

Reactions catalysed: 
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R
UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-538303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 34.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16442 (Residues: 64-354; Coverage: 82%)
Gene name: ABO
Sequence domains: Glycosyltransferase family 6
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 52.58Å b: 149.57Å c: 79.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.209
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Deep evolutionary analysis reveals the design principles of fold A glycosyltransferases.
Taujale et al. (2020)
1 more

1 mention without citation

Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases.
Gagnon et al. (2018)