PDBe 1bv1

X-ray diffraction
2Å resolution

BIRCH POLLEN ALLERGEN BET V 1

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major pollen allergen Bet v 1-A Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.43 KDa
Source organism: Betula pendula
Expression system: Escherichia coli
UniProt:
  • Canonical: P15494 (Residues: 2-160; Coverage: 99%)
Gene names: BETVI, BETVIA
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 32.16Å b: 74.24Å c: 118.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.267
Expression system: Escherichia coli