structure of human KCNQ1-KCNE3-CaM complex with two PIP2. Determined by electron microscopy at 3.9 Å resolution. Released 3 Sept 2025.
Explore 9WD8 in 3D Show helices and sheets RCSB PDB PDBe
9WD8 contains 116 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 | 120-142 | 23 | |
| α-helix | 154-176 | 23 | |
| α-helix | 189-191 | 3 | |
| α-helix | 193-195 | 3 | |
| α-helix | 197-215 | 19 | |
| α-helix | 228-235 | 8 | |
| α-helix | 236-238 | 3 | |
| α-helix | 248-257 | 10 | |
| α-helix | 259-283 | 25 | |
| β-strand | 288 | 1 | 1 |
| β-strand | 294 | 1 | 1 |
| α-helix | 299-310 | 12 | |
| α-helix | 323-354 | 32 | |
| α-helix | 358-372 | 15 | |
| α-helix | 375-382 | 8 | |
| α-helix | 510-530 | 21 | |
| α-helix | 552-555 | 4 | |
| α-helix | 557-561 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-17 | 5 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-50 | 5 | |
| α-helix | 52-56 | 5 | |
| α-helix | 69-73 | 5 | |
| α-helix | 84-91 | 8 | |
| α-helix | 103-110 | 8 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-125 | 7 | |
| α-helix | 139-143 | 5 | |
| α-helix | 146-148 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 58-80 | 23 |
| 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 3 | C, F, I, L | protein | 106 | Homo sapiens | Q9Y6H6 (AlphaFold model) |
| Potassium voltage-gated channel subfamily KQT member 1 | A, D, G, J | protein | 546 | Homo sapiens | P51787 (AlphaFold model) |
>9WD8_1 Calmodulin-1 (chains B, E, H, K) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>9WD8_2 Potassium voltage-gated channel subfamily E member 3 (chains C, F, I, L) METTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLPGRDDNSYMY ILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMISNS
>9WD8_3 Potassium voltage-gated channel subfamily KQT member 1 (chains A, D, G, J) MASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVL VCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFA RKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSV VFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIG YGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASL IQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPG EKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGE TLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMV RIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLH QLLSLH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 8 |
| A1BBG | (2R)-3-{[(S)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy… | C45 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 P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9WD8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.