› 4v3c

X-ray diffraction
1.84Å resolution

The structure of alpha2,3-sialyltransferase variant 2 from Pasteurella dagmatis in complex with the donor product CMP

Released:
DOI: 10.2210/pdb4v3c/pdb
PDB entry 4v3c coloured by chain, front view.
PDB entry 4v3c coloured by chain, side view.
PDB entry 4v3c coloured by chain, top view.
Source organism: Pasteurella dagmatis
Primary publication:
Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by active-site redesign.
Schmölzer K, Czabany T, Luley-Goedl C, Pavkov-Keller T, Ribitsch D, Schwab H, Gruber K, Weber H, Nidetzky B
Chem Commun (Camb) 51 3083-6 (2015)
PMID: 25619424

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialyltransferase Chain: A
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 45.64 KDa
Source organism: Pasteurella dagmatis
Expression system: Escherichia coli
UniProt:
  • Canonical: K9UUI6 (Residues: 2-385; Coverage: 100%)
Sequence domains: Sialyltransferase PMO188
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand C 1 x C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 111.75Å b: 111.75Å c: 65.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.173 0.218
Expression system: Escherichia coli

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Citations

7 review citations

Glycosyltransferases: mechanisms and applications in natural product development.
Liang et al. (2015)
6 more

1 mention without citation

Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.
Hombu et al. (2021)