› 3sxe

X-ray diffraction
1.49Å resolution

Crystal structure of AAAA+UDP+Gal with Glycerol as the cryoprotectant

Released:
DOI: 10.2210/pdb3sxe/pdb
PDB entry 3sxe coloured by chain, front view.
PDB entry 3sxe coloured by chain, side view.
PDB entry 3sxe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Sequence-dependent effects of cryoprotectants on the active sites of the human ABO(H) blood group A and B glycosyltransferases.
Johal AR, Schuman B, Alfaro JA, Borisova S, Seto NO, Evans SV
Acta Crystallogr D Biol Crystallogr 68 268-76 (2012)
PMID: 22349229

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-147725 (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: 34.19 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

3 bound ligands:
Ligand UDP 1 x UDP
Ligand GAL 2 x GAL
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002
Spacegroup: C2221
Unit cell:
a: 52.55Å b: 149.63Å c: 79.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.219
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise Manner.
Gagnon et al. (2015)
5 more

1 mention without citation

Two novel mutations p. L319V and p. L91P in ABO glycosyltransferases lead to Ael and Bel phenotypes.
Lei et al. (2020)