structure of human KCNQ1-KCNE1-CaM complex with PIP2. Determined by electron microscopy at 3.9 Å resolution. Released 20 Aug 2025.
Explore 9VEI in 3D Show helices and sheets RCSB PDB PDBe
9VEI contains 120 α-helices and 8 β-strands across 12 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 | 105-114 | 10 | |
| α-helix | 119-145 | 27 | |
| α-helix | 149-151 | 3 | |
| α-helix | 155-176 | 22 | |
| α-helix | 177-179 | 3 | |
| α-helix | 182-184 | 3 | |
| α-helix | 186-193 | 8 | |
| α-helix | 197-216 | 20 | |
| α-helix | 226-237 | 12 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 259-284 | 26 | |
| α-helix | 299-310 | 12 | |
| α-helix | 323-336 | 14 | |
| α-helix | 338-340 | 3 | |
| α-helix | 342-382 | 41 | |
| α-helix | 507-533 | 27 | |
| α-helix | 552-560 | 9 | |
| α-helix | 588-619 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-18 | 9 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| α-helix | 69-73 | 5 | |
| α-helix | 80-91 | 12 | |
| β-strand | 101-102 | 2 | 1 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 136-137 | 2 | 1 |
| α-helix | 139-146 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-67 | 26 | |
| α-helix | 69-70 | 2 | |
| α-helix | 76-79 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 1 | A, D, G, J | protein | 546 | Homo sapiens | P51787 (AlphaFold model) |
| Calmodulin-1 | B, E, H, K | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
| Potassium voltage-gated channel subfamily E member 1 | C, F, I, L | protein | 129 | Homo sapiens | P15382 (AlphaFold model) |
>9VEI_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, D, G, J) MASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVL VCLIFSVLSTCEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFA RKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSV VFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIG YGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASL IQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPG EKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGE TLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMV RIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLH QLLSLH
>9VEI_2 Calmodulin-1 (chains B, E, H, K) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>9VEI_3 Potassium voltage-gated channel subfamily E member 1 (chains C, F, I, L) MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGCLEALYVLMVLGFFGFFTLG IMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNT HLPETKPSP
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 8 |
| PT5 | [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4… | C47 H85 O19 P3 | 8 |
Mechanisms of KCNQ1 gating modulation by KCNE1/3 for cell-specific function. Cui, C., Zhao, L., Kermani, A.A. et al. Cell Res (2025) 35:876-886. DOI 10.1038/s41422-025-01152-1 · PubMed
Other PDB entries of the same protein (UniProt P51787 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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