structure of human KCNQ1-KCNE1-CaM complex with PIP2. Determined by electron microscopy at 3.36 Å resolution. Released 5 Nov 2025.
Explore 9UC8 in 3D Show helices and sheets RCSB PDB PDBe
9UC8 contains 100 α-helices and 0 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 | 121-142 | 22 | |
| α-helix | 156-174 | 19 | |
| α-helix | 186-194 | 9 | |
| α-helix | 197-217 | 21 | |
| α-helix | 226-238 | 13 | |
| α-helix | 248-257 | 10 | |
| α-helix | 261-283 | 23 | |
| α-helix | 299-310 | 12 | |
| α-helix | 326-335 | 10 | |
| α-helix | 342-344 | 3 | |
| α-helix | 347-351 | 5 | |
| α-helix | 356-385 | 30 | |
| α-helix | 507-532 | 26 | |
| α-helix | 549-575 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| α-helix | 26-35 | 10 | |
| α-helix | 36-39 | 4 | |
| α-helix | 46-57 | 12 | |
| α-helix | 66-74 | 9 | |
| α-helix | 80-93 | 14 | |
| α-helix | 105-112 | 8 | |
| α-helix | 123-131 | 9 | |
| α-helix | 139-148 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 43-62 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 1 | A, D, G, J | protein | 676 | 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 | 30 | Homo sapiens | P15382 (AlphaFold model) |
>9UC8_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, D, G, J) MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPG PAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGW KCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC RSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYA DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKK KKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFM RTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVT QLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLP TYEQLTVPRRGPDEGS
>9UC8_2 Calmodulin-1 (chains B, E, H, K) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>9UC8_3 Potassium voltage-gated channel subfamily E member 1 (chains C, F, I, L) DGKLEALYVLMVLGFFGFFTLGIMLSYIRS
| ID | Name | Formula | Copies |
|---|---|---|---|
| PIO | [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d… | C25 H49 O19 P3 | 8 |
Water and common crystallization additives (K) are not listed.
Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating. Zhong, L., Lin, X., Cheng, X. et al. Cell Res (2025) 35:887-899. DOI 10.1038/s41422-025-01182-9 · 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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