human KCNQ1-CaM-ML277-PIP2 complex in state B. Determined by electron microscopy at 2.5 Å resolution. Released 14 Dec 2022.
Explore 7XNN in 3D Show helices and sheets RCSB PDB PDBe
7XNN contains 104 α-helices and 0 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 | 12-17 | 6 | |
| α-helix | 18-20 | 3 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-54 | 9 | |
| α-helix | 80-82 | 3 | |
| α-helix | 85-92 | 8 | |
| α-helix | 103-110 | 8 | |
| α-helix | 119-127 | 9 | |
| α-helix | 139-146 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 106-114 | 9 | |
| α-helix | 121-141 | 21 | |
| α-helix | 146-148 | 3 | |
| α-helix | 151-176 | 26 | |
| α-helix | 182-184 | 3 | |
| α-helix | 186-194 | 9 | |
| α-helix | 197-211 | 15 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-236 | 13 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-284 | 39 | |
| α-helix | 299-310 | 12 | |
| α-helix | 323-335 | 13 | |
| α-helix | 337-340 | 4 | |
| α-helix | 342-382 | 41 | |
| α-helix | 507-531 | 25 | |
| α-helix | 538-554 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calmodulin-3 | A, D, F, H | protein | 177 | Homo sapiens | P0DP25 (AlphaFold model) |
| Potassium voltage-gated channel subfamily KQT member 1 | B, C, E, G | protein | 692 | Homo sapiens | P51787 (AlphaFold model) |
>7XNN_1 Calmodulin-3 (chains A, D, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
>7XNN_2 Potassium voltage-gated channel subfamily KQT member 1 (chains B, C, E, G) MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPG PAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGW KCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC RSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYA DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKK KKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFM RTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVT QLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLP TYEQLTVPRRGPDEGSLEGGSSGGWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| I0S | (2R)-N-[4-(4-methoxyphenyl)-1,3-thiazol-2-yl]-1-(4-methylbenzene-1-sulfonyl)pip… | C23 H25 N3 O4 S2 | 4 |
| PIO | [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d… | C25 H49 O19 P3 | 4 |
Water and common crystallization additives (K) are not listed.
Structural mechanisms for the activation of human cardiac KCNQ1 channel by electro-mechanical coupling enhancers. Ma, D., Zhong, L., Yan, Z. et al. Proc Natl Acad Sci U S A (2022) 119:e2207067119-e2207067119. DOI 10.1073/pnas.2207067119 · PubMed
Other PDB entries of the same protein (UniProt P0DP25 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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