2ii6

X-ray diffraction
1.75Å resolution

Crystal structure of Pasteurella multocida sialyltransferase D141N mutant in open conformation with CMP bound

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

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 Chain: A
Molecule details ›
Chain: A
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: SSRL BEAMLINE BL1-5
Spacegroup: P21
Unit cell:
a: 52.625Å b: 62.049Å c: 61.529Å
α: 90° β: 113.7° γ: 90°
R-values:
R R work R free
0.203 0.2 0.247
Expression system: Escherichia coli BL21(DE3)