NMR structure of interleukin-13. Determined by solution NMR. Released 4 Jul 2001.
Explore 1GA3 in 3D Show helices and sheets RCSB PDB PDBe
1GA3 contains 4 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 | 8-21 | 14 | |
| β-strand | 34-35 | 2 | 1 |
| α-helix | 44-51 | 8 | |
| α-helix | 61-68 | 8 | |
| β-strand | 89-90 | 2 | 1 |
| α-helix | 92-109 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-13 | A | protein | 113 | Homo sapiens | P35225 (AlphaFold model) |
>1GA3_1 Interleukin-13 (chains A) GGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAI EKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN
Solution structure of interleukin-13 and insights into receptor engagement. Eisenmesser, E.Z., Horita, D.A., Altieri, A.S. et al. J Mol Biol (2001) 310:231-241. DOI 10.1006/jmbi.2001.4765 · PubMed
Other PDB entries of the same protein (UniProt P35225 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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