human KCNQ1-CaM-ML277-PIP2 complex in state A. Determined by electron microscopy at 3.1 Å resolution. Released 14 Dec 2022.
Explore 7XNL in 3D Show helices and sheets RCSB PDB PDBe
7XNL contains 116 α-helices and 8 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 | 105-114 | 10 | |
| α-helix | 121-142 | 22 | |
| α-helix | 146-148 | 3 | |
| α-helix | 149-177 | 29 | |
| α-helix | 178-180 | 3 | |
| α-helix | 187-193 | 7 | |
| α-helix | 197-216 | 20 | |
| α-helix | 224-236 | 13 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 259-284 | 26 | |
| α-helix | 299-310 | 12 | |
| α-helix | 323-335 | 13 | |
| α-helix | 337-339 | 3 | |
| α-helix | 342-360 | 19 | |
| α-helix | 367-385 | 19 | |
| α-helix | 390-394 | 5 | |
| α-helix | 510-532 | 23 | |
| α-helix | 538-562 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| α-helix | 66-74 | 9 | |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103-112 | 10 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-128 | 10 | |
| β-strand | 136-138 | 3 | 1 |
| α-helix | 139-146 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 1 | A, C, E, G | protein | 692 | Homo sapiens | P51787 (AlphaFold model) |
| Calmodulin-3 | B, D, F, H | protein | 177 | Homo sapiens | P0DP25 (AlphaFold model) |
>7XNL_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, C, E, G) MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPG PAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGW KCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC RSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYA DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKK KKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFM RTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVT QLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLP TYEQLTVPRRGPDEGSLEGGSSGGWSHPQFEK
>7XNL_2 Calmodulin-3 (chains B, D, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
| 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 P51787 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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