NMR structure of human KCNE1 in LMPG micelles at pH 6.0 and 40 degree C. Determined by solution NMR. Released 9 Dec 2008.
Explore 2K21 in 3D Show helices and sheets RCSB PDB PDBe
2K21 contains 7 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 | 4-9 | 6 | |
| α-helix | 13-22 | 10 | |
| α-helix | 30-32 | 3 | |
| α-helix | 46-71 | 26 | |
| α-helix | 92-105 | 14 | |
| α-helix | 121-124 | 4 | |
| α-helix | 126-128 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily E member | A | protein | 138 | Homo sapiens | P15382 (AlphaFold model) |
>2K21_1 Potassium voltage-gated channel subfamily E member (chains A) MGHHHHHHGMILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSGDGKLEALYVLMVL GFFGFFTLGIMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYKSCYVVEN HLAIEQPNTHLPETKPSP
Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. Kang, C., Tian, C., Sonnichsen, F.D. et al. Biochemistry (2008) 47:7999-8006. DOI 10.1021/bi800875q · PubMed
Other PDB entries of the same protein (UniProt P15382 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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