2iiq

X-ray diffraction
2.3Å resolution

Crystal structure of Pasteurella multocida sialyltransferase in an open conformation with CMP bound

Released:
Source organism: Pasteurella multocida
Entry authors: Ni L, Fisher AJ

Function and Biology Details

Reaction catalysed:
CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 52.528Å b: 61.572Å c: 119.547Å
α: 90° β: 94.77° γ: 90°
R-values:
R R work R free
0.21 0.208 0.256
Expression system: Escherichia coli BL21(DE3)