structure of human KCNQ1-KCNE1-CaM complex. Determined by electron microscopy at 2.7 Å resolution. Released 20 Aug 2025.
Explore 9VEC in 3D Show helices and sheets RCSB PDB PDBe
9VEC contains 116 α-helices and 16 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 | 107-114 | 8 | |
| α-helix | 122-142 | 21 | |
| α-helix | 169-177 | 9 | |
| α-helix | 178-180 | 3 | |
| α-helix | 186-194 | 9 | |
| α-helix | 197-215 | 19 | |
| α-helix | 225-228 | 4 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 259-284 | 26 | |
| α-helix | 299-310 | 12 | |
| α-helix | 323-357 | 35 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-366 | 3 | |
| α-helix | 368-383 | 16 | |
| α-helix | 392-395 | 4 | |
| α-helix | 508-532 | 25 | |
| α-helix | 538-567 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-21 | 13 | |
| β-strand | 28 | 1 | 3 |
| α-helix | 30-38 | 9 | |
| α-helix | 46-53 | 8 | |
| β-strand | 64 | 1 | 3 |
| α-helix | 66-73 | 8 | |
| α-helix | 80-91 | 12 | |
| β-strand | 100-102 | 3 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-126 | 8 | |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 139-148 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 43-64 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 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) |
| Potassium voltage-gated channel subfamily KQT member 1 | A, D, G, J | protein | 546 | Homo sapiens | P51787 (AlphaFold model) |
>9VEC_1 Calmodulin-1 (chains B, E, H, K) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>9VEC_2 Potassium voltage-gated channel subfamily E member 1 (chains C, F, I, L) MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGCLEALYVLMVLGFFGFFTLG IMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNT HLPETKPSP
>9VEC_3 Potassium voltage-gated channel subfamily KQT member 1 (chains A, D, G, J) MASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVL VCLIFSVLSTCEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFA RKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSV VFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIG YGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASL IQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPG EKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGE TLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMV RIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLH QLLSLH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 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 P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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