Unraveling the structure of interleukin-2: reply. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 Oct 1993.
Explore 3INK in 3D Show helices and sheets RCSB PDB PDBe
3INK contains 17 α-helices and 4 β-strands across 2 chains. 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 | 7-28 | 22 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-70 | 8 | |
| α-helix | 75-77 | 3 | |
| α-helix | 82-96 | 15 | |
| β-strand | 107-112 | 6 | 1 |
| α-helix | 114-129 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-28 | 22 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44 | 1 | 2 |
| α-helix | 45-47 | 3 | |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-70 | 8 | |
| α-helix | 75-77 | 3 | |
| α-helix | 82-96 | 15 | |
| β-strand | 112 | 1 | 2 |
| α-helix | 114-132 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-2 | C, D | protein | 133 | Homo sapiens | P60568 (AlphaFold model) |
>3INK_1 INTERLEUKIN-2 (chains C, D) APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLE EELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR WITFAQSIISTLT
Response. McKay, D.B. Science (1992) 257:412-413. DOI 10.1126/science.257.5068.412 · PubMed
Other PDB entries of the same protein (UniProt P60568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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