Solution Structure of the Carboxyl Terminal Domain of the Ciliary Neurotrophic Factor Receptor. Determined by solution NMR. Released 10 Aug 2004.
Explore 1UC6 in 3D Show helices and sheets RCSB PDB PDBe
1UC6 contains 2 α-helices and 9 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 | 8-11 | 4 | |
| β-strand | 12-18 | 7 | 1 |
| α-helix | 19 | 1 | |
| β-strand | 26-31 | 6 | 1 |
| β-strand | 44 | 1 | 2 |
| β-strand | 46-52 | 7 | 3 |
| β-strand | 61-63 | 3 | 3 |
| β-strand | 68-71 | 4 | 1 |
| β-strand | 80-85 | 6 | 3 |
| β-strand | 88 | 1 | 2 |
| β-strand | 99-103 | 5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ciliary Neurotrophic Factor Receptor alpha | A | protein | 109 | Homo sapiens | P26992 (AlphaFold model) |
>1UC6_1 Ciliary Neurotrophic Factor Receptor alpha (chains A) GPLGSVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQH VELSNGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEE
Solution structure of the C-terminal domain of the ciliary neurotrophic factor (CNTF) receptor and ligand free associations among components of the CNTF receptor complex. Man, D., He, W., Sze, K.H. et al. J Biol Chem (2003) 278:23285-23294. DOI 10.1074/jbc.M301976200 · PubMed
Other PDB entries of the same protein (UniProt P26992 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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