› 4a8v

X-ray diffraction
1.23Å resolution

Crystal Structure of Birch Pollen Allergen Bet v 1 isoform j in complex with 8-Anilinonaphthalene-1-sulfonate (ANS)

Released:
DOI: 10.2210/pdb4a8v/pdb
PDB entry 4a8v coloured by chain, front view.
PDB entry 4a8v coloured by chain, side view.
PDB entry 4a8v coloured by chain, top view.
Source organism: Betula pendula
Primary publication:
Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen bet v 1.
Kofler S, Asam C, Eckhard U, Wallner M, Ferreira F, Brandstetter H
OpenAccess logo J Mol Biol 422 109-23 (2012)
PMID: 22634284

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major pollen allergen Bet v 1-J Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.43 KDa
Source organism: Betula pendula
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43183 (Residues: 2-160; Coverage: 99%)
Gene name: BETV1J
Sequence domains: Pathogenesis-related protein Bet v 1 family
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

4 bound ligands:
Ligand 2AN 1 x 2AN
Ligand MPD 2 x MPD
Ligand SO4 4 x SO4
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 32.76Å b: 56Å c: 38.08Å
α: 90° β: 93.4° γ: 90°
R-values:
R R work R free
0.137 0.135 0.171
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

Structural and functional aspects of PR-10 proteins.
Fernandes et al. (2013)
15 more

4 mentions without citation

Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family.
Aglas et al. (2020)
3 more