Structure of Xenopus KCNQ1-CaM in GDN. Determined by electron microscopy at 3.46 Å resolution. Released 15 Oct 2025.
Explore 9MY3 in 3D Show helices and sheets RCSB PDB PDBe
9MY3 contains 116 α-helices and 16 β-strands across 8 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 | 96-105 | 10 | |
| α-helix | 110-134 | 25 | |
| α-helix | 139-167 | 29 | |
| α-helix | 168-170 | 3 | |
| α-helix | 177-183 | 7 | |
| α-helix | 187-204 | 18 | |
| α-helix | 217-226 | 10 | |
| α-helix | 227-230 | 4 | |
| α-helix | 236-247 | 12 | |
| α-helix | 249-274 | 26 | |
| α-helix | 289-300 | 12 | |
| α-helix | 313-326 | 14 | |
| α-helix | 328-347 | 20 | |
| α-helix | 348-350 | 3 | |
| α-helix | 351-353 | 3 | |
| α-helix | 354-357 | 4 | |
| α-helix | 358-373 | 16 | |
| α-helix | 380-383 | 4 | |
| α-helix | 499-520 | 22 | |
| α-helix | 524-525 | 2 | |
| α-helix | 527-553 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-20 | 8 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 66-74 | 9 | |
| α-helix | 80-91 | 12 | |
| β-strand | 100-102 | 3 | 2 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-128 | 10 | |
| β-strand | 136-138 | 3 | 2 |
| α-helix | 139-145 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 1 | A, C, E, G | protein | 545 | Xenopus laevis | P70057 (AlphaFold model) |
| Calmodulin-1 | B, D, F, H | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
>9MY3_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, C, E, G) MATDPPRPTINLDPRVSIYSGRRPLLSRTNIQGRVYNFLERPTGWKCFVYHFTVFLIVLI CLIFSVLSTIQQYNNLATETLFWMEIVLVVFFGAEYVVRLWSAGCRSKYVGVWGRLRFAR KPISVIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVV FIHRQELITTLYIGFLGLIFSSYFVYLAEKDAIDSSGEYQFGSYADALWWGVVTVTTIGY GDKVPQTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLI QTAWRCYAAENPDSATWKIYIRKQSRNHHLMSPSPKPKKSAMVKKKKIRTERDEGSTDKM LNIPHITYDHVADDRKNDGYSVESYENTVRKPFGFLDPSTGPFIRTSSFTDDLDMEGDTL LTPITHISELKEHHRAAIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRI KELQRRLDQSLGKPSLFLSVSDKVKDKGINTIGSRLNRVEDKVTQMDHKLNLITDMLHHL LTNQQ
>9MY3_2 Calmodulin-1 (chains B, D, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
A physiologically-relevant intermediate state structure of a voltage-gated potassium channel. Kyriakis, E., Sastre, D., Eldstrom, J. et al. Nat Commun (2025) 16:8814-8814. DOI 10.1038/s41467-025-64060-3 · PubMed
Other PDB entries of the same protein (UniProt P70057 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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