Xenopus KCNQ1 Intermediate State (E1R/R2E) in complex with UCL2077. Determined by electron microscopy at 3.95 Å resolution. Released 2 Sept 2026.
Explore 10NK in 3D Show helices and sheets RCSB PDB PDBe
10NK contains 106 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 | 98-104 | 7 | |
| α-helix | 110-136 | 27 | |
| α-helix | 140-162 | 23 | |
| α-helix | 163-167 | 5 | |
| α-helix | 172-174 | 3 | |
| α-helix | 177-184 | 8 | |
| α-helix | 187-204 | 18 | |
| α-helix | 217-229 | 13 | |
| α-helix | 236-274 | 39 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-300 | 12 | |
| α-helix | 313-329 | 17 | |
| α-helix | 331-346 | 16 | |
| α-helix | 357-372 | 16 | |
| α-helix | 373-375 | 3 | |
| α-helix | 380-383 | 4 | |
| α-helix | 498-521 | 24 | |
| α-helix | 527-548 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 14-17 | 4 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 30-37 | 8 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 66-74 | 9 | |
| α-helix | 80-92 | 13 | |
| β-strand | 101 | 1 | 2 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-127 | 9 | |
| β-strand | 137 | 1 | 2 |
| α-helix | 139-145 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-17 | 4 | |
| β-strand | 27-28 | 2 | 3 |
| α-helix | 30-38 | 9 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 66-74 | 9 | |
| α-helix | 80-91 | 12 | |
| β-strand | 100-101 | 2 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-128 | 10 | |
| β-strand | 137-138 | 2 | 4 |
| α-helix | 139-143 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 96-105 | 10 | |
| α-helix | 110-134 | 25 | |
| α-helix | 137-141 | 5 | |
| α-helix | 143-167 | 25 | |
| α-helix | 168-170 | 3 | |
| α-helix | 172-174 | 3 | |
| α-helix | 176-183 | 8 | |
| α-helix | 187-204 | 18 | |
| α-helix | 217-229 | 13 | |
| α-helix | 237-247 | 11 | |
| α-helix | 249-273 | 25 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-299 | 11 | |
| α-helix | 313-346 | 34 | |
| α-helix | 357-375 | 19 | |
| α-helix | 498-522 | 25 | |
| α-helix | 527-548 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin-1 | B, C, D, E | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
| Potassium voltage-gated channel subfamily KQT member 1 | A, F, G, H | protein | 545 | Xenopus laevis | P70057 (AlphaFold model) |
>10NK_1 Calmodulin-1 (chains B, C, D, E) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>10NK_2 Potassium voltage-gated channel subfamily KQT member 1 (chains A, F, G, H) MATDPPRPTINLDPRVSIYSGRRPLLSRTNIQGRVYNFLERPTGWKCFVYHFTVFLIVLI CLIFSVLSTIQQYNNLATETLFWMRIVLVVFFGAEYVVRLWSAGCRSKYVGVWGRLRFAR KPISVIDLIVVVASVIVLCVGSNGQVFATSAIRGIEFLQILRMLHVDRQGGTWRLLGSVV FIHRQELITTLYIGFLGLIFSSYFVYLAEKDAIDSSGEYQFGSYADALWWGVVTVTTIGY GDKVPQTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLI QTAWRCYAAENPDSATWKIYIRKQSRNHHLMSPSPKPKKSAMVKKKKIRTERDEGSTDKM LNIPHITYDHVADDRKNDGYSVESYENTVRKPFGFLDPSTGPFIRTSSFTDDLDMEGDTL LTPITHISELKEHHRAAIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRI KELQRRLDQSLGKPSLFLSVSDKVKDKGINTIGSRLNRVEDKVTQMDHKLNLITDMLHHL LTNQQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1C6W | 1,1,1-triphenyl-N-[(pyridin-3-yl)methyl]methanamine | C25 H22 N2 | 2 |
Structural and kinetic mechanisms of state-dependent potassium channel inhibition. Kyriakis, E., Roscioni, A., Eldstrom, J. et al. Sci Adv (2026).
Other PDB entries of the same protein (UniProt P0DP23 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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