4c2s

X-ray diffraction
2.48Å resolution

Crystal structure of the fucosylgalactoside alpha N- acetylgalactosaminyltransferase (GTA P156L mutant) in complex with UDP and deoxy-H-antigen acceptor

Released:
Source organism: Homo sapiens
Entry authors: Weadge JT, Palcic M, Henriksen A

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-147726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 34.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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

Carbohydrate polymer : NEW Components: DLG, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: C2
Unit cell:
a: 147.51Å b: 52.61Å c: 80.27Å
α: 90° β: 89.97° γ: 90°
R-values:
R R work R free
0.147 0.145 0.182
Expression system: Escherichia coli BL21