Crystal structure of OPTN E50K mutant and TBK1 complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 28 Sept 2016.
Explore 5EOA in 3D Show helices and sheets RCSB PDB PDBe
5EOA contains 4 α-helices and 0 β-strands across 4 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 | 37-98 | 62 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-101 | 65 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 680-714 | 35 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 683-717 | 35 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Optineurin | A, B | protein | 82 | Homo sapiens | Q96CV9 (AlphaFold model) |
| Serine/threonine-protein kinase TBK1 | C, D | protein | 57 | Homo sapiens | Q9UHD2 (AlphaFold model) |
>5EOA_1 Optineurin (chains A, B) GPGSHLAHPNLDTFTPEELLQQMKELLTKNHQLKEAMKLNNQAMKGRFEELSAWTEKQKE ERQFFEIQSKEAKERLMALSHE
>5EOA_2 Serine/threonine-protein kinase TBK1 (chains C, D) GPGSYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL
Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins. Li, F., Xie, X., Wang, Y. et al. Nat Commun (2016) 7:12708-12708. DOI 10.1038/ncomms12708 · PubMed
Other PDB entries of the same protein (UniProt Q96CV9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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