PDBe 4fqw

X-ray diffraction
2.02Å resolution

Crystal Structure of AAAA+UDP+Gal at pH 5.0 with MPD as the cryoprotectant

Released:

Function and Biology Details

Reactions catalysed:
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
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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 34.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16442 (Residues: 64-354; Coverage: 82%)
Gene name: ABO
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002
Spacegroup: C2221
Unit cell:
a: 52.3Å b: 149.22Å c: 79.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.191 0.258
Expression system: Escherichia coli