PDBe 1ro7

X-ray diffraction
1.8Å resolution

Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-2,3/8-sialyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 259 amino acids
Theoretical weight: 30.73 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9LAK3 (Residues: 1-259; Coverage: 89%)
Gene name: cst-II
Structure domains: sialyltransferase cstii, chain A

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21
Unit cell:
a: 83.66Å b: 66.031Å c: 99.172Å
α: 90° β: 94.42° γ: 90°
R-values:
R R work R free
0.217 0.217 0.248
Expression system: Escherichia coli BL21