Solution structure of human interleukin-21. Determined by solution NMR. Released 19 Jun 2007.
Explore 2OQP in 3D Show helices and sheets RCSB PDB PDBe
2OQP contains 9 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 | 6-23 | 18 | |
| α-helix | 25-27 | 3 | |
| β-strand | 33-34 | 2 | 1 |
| α-helix | 44-48 | 5 | |
| α-helix | 50-53 | 4 | |
| α-helix | 65-75 | 11 | |
| α-helix | 77-79 | 3 | |
| β-strand | 102-103 | 2 | 1 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| α-helix | 121-124 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-21 | A | protein | 134 | Homo sapiens | Q9HBE4 (AlphaFold model) |
>2OQP_1 Interleukin-21 (chains A) MQGQDRHMIRMRQLIDIVDQLKNYVNDLVPEFLPAPEDVETNCEWSAFSCFQKAQLKSAN TGNNERIINVSIKKLKRKPPSTNAGRRQKHRLTCPSCDSYEKKPPKEFLERFKSLLQKMI HQHLSSRTHGSEDS
The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue. Bondensgaard, K., Breinholt, J., Madsen, D. et al. J Biol Chem (2007) 282:23326-23336. DOI 10.1074/jbc.M701313200 · PubMed
Other PDB entries of the same protein (UniProt Q9HBE4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2OQP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.