2ex0

X-ray diffraction
1.65Å resolution

Crystal structure of multifunctional sialyltransferase from Pasteurella Multocida

Released:

Function and Biology Details

Reaction catalysed:
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-172445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-2,3/2,6-sialyltransferase/sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 46.47 KDa
Source organism: Pasteurella multocida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15KI8 (Residues: 26-412; Coverage: 94%)
Sequence domains: Sialyltransferase PMO188
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 63.718Å b: 61.281Å c: 96.649Å
α: 90° β: 101.56° γ: 90°
R-values:
R R work R free
0.196 0.193 0.218
Expression system: Escherichia coli BL21(DE3)