1bv1 Summary



The structure was published by Gajhede, M., Osmark, P., Poulsen, F.M., et al., Schou, C., Lowenstein, H., and Spangfort, M.D., in 1996 in a paper entitled "X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1997.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of BET V 1. This molecule has the UniProt identifier P15494 (BEV1A_BETPN)search. The sample contained 159 residues which is 99% of the natural sequence. Out of 159 residues 159 were observed and are deposited in the PDB.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A BET V 1 P15494 (2-160) (BEV1A_BETPN)search Betula pendulasearch 99% 159 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15494 (2 - 160) BET V 1 Betula pendula

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P15494) Pathogenesis-related protein 10 (PR10)-likesearch Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4search PF00407: Pathogenesis-related protein Bet v I familysearch

Chain ID Cellular component (GO) Biological process (GO)
A (P15494) cytoplasmsearch response to biotic stimulussearch defense responsesearch

Chain InterPro annotation
A Bet v I domainsearch START-like domainsearch Bet v I type allergensearch