4Z3L

CRYSTAL STRUCTURE OF BIRCH POLLEN ALLERGEN BET V 1 MUTANT G26L, D69I, P90L, K97I

Summary for 4Z3L

DescriptorMajor pollen allergen Bet v 1-A, SULFATE ION (3 entities in total)
Functional Keywordsallergen, fold stability
Biological sourceBetula pendula (European white birch)
Cellular locationCytoplasm P15494
Total number of polymer chains6
Total molecular weight106439.62
Authors
Freier, R.,Brandstetter, H. (deposition date: 2015-03-31, release date: 2015-11-25, Last modification date: 2016-05-18)
Primary citation
Machado, Y.,Freier, R.,Scheiblhofer, S.,Thalhamer, T.,Mayr, M.,Briza, P.,Grutsch, S.,Ahammer, L.,Fuchs, J.E.,Wallnoefer, H.G.,Isakovic, A.,Kohlbauer, V.,Hinterholzer, A.,Steiner, M.,Danzer, M.,Horejs-Hoeck, J.,Ferreira, F.,Liedl, K.R.,Tollinger, M.,Lackner, P.,Johnson, C.M.,Brandstetter, H.,Thalhamer, J.,Weiss, R.
Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen.
J.Allergy Clin.Immunol., 137:1525-1534, 2016
PubMed: 26559323 (PDB entries with the same primary citation)
DOI: 10.1016/j.jaci.2015.09.026
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.5 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.25513 0.2% 8.5% 2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171588
PDB entries from 2020-11-25