2B91: Interleukin-4 variant F82DR85A

Crystal structure of the interleukin-4 variant F82DR85A. Determined by X-ray diffraction at 2.0 Å resolution. Released 30 May 2006.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,182
Mol. weight
15.16 kDa
Released
30 May 2006

Explore 2B91 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2B91 contains 5 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix6-1712
β-strand28-3031
α-helix32-343
α-helix41-5919
α-helix70-9425
β-strand106-10831
α-helix109-12719

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interleukin-4Aprotein129Homo sapiensP05112 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2B91_1 Interleukin-4 (chains A)
HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHE
KDTRCLGATAQQFHRHKQLIRDLKALDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIM
REKYSKCSS

Primary citation

A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor. Kraich, M., Klein, M., Patino, E. et al. BMC Biol (2006) 4:13-13. DOI 10.1186/1741-7007-4-13 · PubMed

Other PDB entries of the same protein (UniProt P05112 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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