Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Dec 2002.
Explore 1NBP in 3D Show helices and sheets RCSB PDB PDBe
1NBP contains 9 α-helices and 4 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 | 7-28 | 22 | |
| α-helix | 33-39 | 7 | |
| 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 | |
| α-helix | 104-106 | 3 | |
| β-strand | 107 | 1 | 2 |
| α-helix | 108 | 1 | |
| β-strand | 112 | 1 | 1 |
| α-helix | 114-129 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-2 | A | protein | 133 | Homo sapiens | P60568 (AlphaFold model) |
>1NBP_1 Interleukin-2 (chains A) APTSSSTKKTQLQLEHLLLDLQMILNGINNCKNPKLTRMLTFKFYMPKKATELKHLQCLE EELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR WITFCQSIISTLT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MHC | 3-mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one | C14 H16 N2 O S | 1 |
Water and common crystallization additives (SO4) are not listed.
Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2. Hyde, J., Braisted, A.C., Randal, M. et al. Biochemistry (2003) 42:6475-6483. DOI 10.1021/bi034138g · 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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