X-ray diffraction
2.1Å resolution

Crystal structure of doubly spin labelled VcSiaP R125


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Sialic acid-binding periplasmic protein SiaP Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 37.33 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
  • Canonical: Q9KR64 (Residues: 22-321; Coverage: 100%)
Gene names: VC_1779, siaP
Sequence domains: Bacterial extracellular solute-binding protein, family 7
Structure domains: Bacterial extracellular solute-binding protein, family 7

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.3
Unit cell:
a: 72.27Å b: 78.1Å c: 116.24Å
α: 90° β: 90° γ: 90°
R R work R free
0.221 0.219 0.262
Expression system: Escherichia coli