› 2wgz

X-ray diffraction
2.12Å resolution

Crystal structure of alpha-1,3 galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNP-beta-Gal)

Released:
DOI: 10.2210/pdb2wgz/pdb
PDB entry 2wgz coloured by chain, front view.
PDB entry 2wgz coloured by chain, side view.
PDB entry 2wgz coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of alpha-1,3-galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNPbetaGal).
Jamaluddin H, Tumbale P, Ferns TA, Thiyagarajan N, Brew K, Acharya KR
Biochem Biophys Res Commun 385 601-4 (2009)
PMID: 19486884

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-537696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyllactosaminide alpha-1,3-galactosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 290 amino acids
Theoretical weight: 34.25 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14769 (Residues: 80-368; Coverage: 79%)
Gene name: GGTA1
Sequence domains: Glycosyltransferase family 6
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

6 bound ligands:
Ligand 147 1 x 147
Ligand MN 2 x MN
Ligand UDP 2 x UDP
Ligand GOL 6 x GOL
Ligand GAL 1 x GAL
Ligand NPO 1 x NPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 45.146Å b: 94.222Å c: 94.465Å
α: 90° β: 99.05° γ: 90°
R-values:
R R work R free
0.17 0.169 0.206
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Crossroads between Bacterial and Mammalian Glycosyltransferases.
Brockhausen I. (2014)
1 other article