› 4wfv

X-ray diffraction
1.4Å resolution

Bovine allergen Bos d 2 in the monoclinic space group C2.

Released:
DOI: 10.2210/pdb4wfv/pdb
PDB entry 4wfv coloured by chain, front view.
PDB entry 4wfv coloured by chain, side view.
PDB entry 4wfv coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Dimerization of lipocalin allergens.
Niemi MH, Rytkönen-Nissinen M, Miettinen I, Jänis J, Virtanen T, Rouvinen J
Sci Rep 5 13841 (2015)
PMID: 26346541

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173306 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Allergen Bos d 2 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 17.87 KDa
Source organism: Bos taurus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q28133 (Residues: 17-172; Coverage: 100%)
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 125.94Å b: 36.59Å c: 36.47Å
α: 90° β: 95.86° γ: 90°
R-values:
R R work R free
0.197 0.196 0.214
Expression system: Komagataella pastoris

Quick links

Citations

6 review citations

Tuning IgE: IgE-Associating Molecules and Their Effects on IgE-Dependent Mast Cell Reactions.
Ando et al. (2021)
5 more

3 mentions without citation

Dimerization of lipocalin allergens.
Niemi et al. (2015)
2 more