Interleukin-4 (wild-type). Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Jan 1996.
Explore 1HIK in 3D Show helices and sheets RCSB PDB PDBe
1HIK contains 6 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 | 6-17 | 12 | |
| α-helix | 23-26 | 4 | |
| β-strand | 28-30 | 3 | 1 |
| α-helix | 41-59 | 19 | |
| α-helix | 63-66 | 4 | |
| α-helix | 70-94 | 25 | |
| β-strand | 106-108 | 3 | 1 |
| α-helix | 109-126 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-4 | A | protein | 129 | Homo sapiens | P05112 (AlphaFold model) |
>1HIK_1 INTERLEUKIN-4 (chains A) HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHE KDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIM REKYSKCSS
Human interleukin-4 and variant R88Q: phasing X-ray diffraction data by molecular replacement using X-ray and nuclear magnetic resonance models. Muller, T., Oehlenschlager, F., Buehner, M. J Mol Biol (1995) 247:360-372. DOI 10.1006/jmbi.1994.0144 · 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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