Crystal Structure of Human Interleukin-2 Complexed with SP-1985. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Jul 2002.
Explore 1M49 in 3D Show helices and sheets RCSB PDB PDBe
1M49 contains 16 α-helices and 8 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 | 5-28 | 24 | |
| α-helix | 33-40 | 8 | |
| β-strand | 44 | 1 | 1 |
| β-strand | 47 | 1 | 2 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-72 | 10 | |
| α-helix | 82-97 | 16 | |
| β-strand | 107 | 1 | 2 |
| β-strand | 112 | 1 | 1 |
| α-helix | 114-131 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-28 | 24 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44 | 1 | 3 |
| β-strand | 47 | 1 | 4 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-72 | 10 | |
| α-helix | 82-96 | 15 | |
| α-helix | 104-106 | 3 | |
| β-strand | 107 | 1 | 4 |
| α-helix | 108 | 1 | |
| β-strand | 112 | 1 | 3 |
| α-helix | 114-131 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| interleukin-2 | A, B | protein | 133 | Homo sapiens | P60568 (AlphaFold model) |
>1M49_1 interleukin-2 (chains A, B) APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLE EELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR WITFCQSIISTLT
| ID | Name | Formula | Copies |
|---|---|---|---|
| CMM | 2-[2-(1-carbamimidoyl-piperidin-3-yl)-acetylamino]-3-{4-[2-(3-oxalyl-1H-indol-7… | C30 H35 N5 O6 | 2 |
Binding of small molecules to an adaptive protein-protein interface. Arkin, M.A., Randal, M., DeLano, W.L. et al. Proc Natl Acad Sci U S A (2003) 100:1603-1608. DOI 10.1073/pnas.252756299 · 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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