Structural Basis for KCNE3 and Estrogen Modulation of the KCNQ1 Channel. Determined by solution NMR. Released 21 Sept 2016.
Explore 2NDJ in 3D Show helices and sheets RCSB PDB PDBe
2NDJ contains 6 α-helices and 0 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 | 2-4 | 3 | |
| α-helix | 8-29 | 22 | |
| α-helix | 32-34 | 3 | |
| α-helix | 55-77 | 23 | |
| α-helix | 78-82 | 5 | |
| α-helix | 85-87 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily E member 3 | A | protein | 112 | Homo sapiens | Q9Y6H6 (AlphaFold model) |
>2NDJ_1 Potassium voltage-gated channel subfamily E member 3 (chains A) MGHHHHHHGMETTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLP GRDDNSYMYILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMI
Structural basis for KCNE3 modulation of potassium recycling in epithelia. Kroncke, B.M., Van Horn, W.D., Smith, J. et al. Sci Adv (2016) 2:e1501228-e1501228. DOI 10.1126/sciadv.1501228 · PubMed
Other PDB entries of the same protein (UniProt Q9Y6H6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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