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› 5cqp

X-ray diffraction
1.83Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.41 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 HG 4 x HG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 52.72Å b: 149.22Å c: 79.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.217
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Park et al. (2018)
4 more