Crystal structure of the interleukin-4 variant T13DR85A. Determined by X-ray diffraction at 2.1 Å resolution. Released 30 May 2006.
Explore 2B90 in 3D Show helices and sheets RCSB PDB PDBe
2B90 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-18 | 13 | |
| β-strand | 28-30 | 3 | 1 |
| α-helix | 32-34 | 3 | |
| α-helix | 41-59 | 19 | |
| α-helix | 70-94 | 25 | |
| β-strand | 106-108 | 3 | 1 |
| α-helix | 109-127 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-4 | A | protein | 129 | Homo sapiens | P05112 (AlphaFold model) |
>2B90_1 Interleukin-4 (chains A) HKCDITLQEIIKDLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHE KDTRCLGATAQQFHRHKQLIRFLKALDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIM REKYSKCSS
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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