4MNS

Crystal structure of the major pollen allergen Bet v 1-A in complex with P303

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.160 
  • R-Value Work: 0.131 
  • R-Value Observed: 0.133 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history. 


Literature

Development and evaluation of a sublingual tablet based on recombinant Bet v 1 in birch pollen-allergic patients.

Nony, E., Bouley, J., Le Mignon, M., Lemoine, P., Jain, K., Horiot, S., Mascarell, L., Pallardy, M., Vincentelli, R., Leone, P., Roussel, A., Batard, T., Abiteboul, K., Robin, B., de Beaumont, O., Arvidsson, M., Rak, S., Moingeon, P.

(2015) Allergy 70: 795-804

  • DOI: https://doi.org/10.1111/all.12622
  • Primary Citation of Related Structures:  
    4MNS

  • PubMed Abstract: 

    Sublingual immunotherapy (SLIT) applied to type I respiratory allergies is commonly performed with natural allergen extracts. Herein, we developed a sublingual tablet made of pharmaceutical-grade recombinant Bet v 1.0101 (rBet v 1) and investigated its clinical safety and efficacy in birch pollen (BP)-allergic patients.

    • Organizational Affiliation: 

    Stallergenes, Antony, France.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major pollen allergen Bet v 1-A159Betula pendulaMutation(s): 0 
Gene Names: BETVIA, BETVI
UniProt
Find proteins for P15494 (Betula pendula)
Explore P15494 
Go to UniProtKB:  P15494
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15494
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
2AX
Query on 2AX
Download Ideal Coordinates CCD File 
B [auth A](3R,4R,5aR,11aR)-3-methyl-6,11-dioxo-2,3,4,5,5a,6,11,11a-octahydrothiepino[3,2-g]isoquinoline-4-carboxylic acid
C15 H15 N O4 S
BHJMBPMSJMEWOB-MWMDWWONSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.160 
  • R-Value Work: 0.131 
  • R-Value Observed: 0.133 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 39.928α = 90
b = 58.577β = 90
c = 58.767γ = 90
Software Package:
Software NamePurpose
DNAdata collection
AMoREphasing
REFMACrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-03-11
    Type: Initial release
  • Version 1.1: 2015-04-15
    Changes: Database references
  • Version 1.2: 2015-04-22
    Changes: Database references
  • Version 1.3: 2015-07-01
    Changes: Database references
  • Version 1.4: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description