human KCNQ1-CaM in apo state. Determined by electron microscopy at 3.5 Å resolution. Released 14 Dec 2022.
Explore 7XNI in 3D Show helices and sheets RCSB PDB PDBe
7XNI contains 108 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 | 105-115 | 11 | |
| α-helix | 120-142 | 23 | |
| α-helix | 149-177 | 29 | |
| α-helix | 178-180 | 3 | |
| α-helix | 187-193 | 7 | |
| α-helix | 197-215 | 19 | |
| α-helix | 224-236 | 13 | |
| α-helix | 237-241 | 5 | |
| α-helix | 248-257 | 10 | |
| α-helix | 259-284 | 26 | |
| α-helix | 299-310 | 12 | |
| α-helix | 323-361 | 39 | |
| α-helix | 367-384 | 18 | |
| α-helix | 390-394 | 5 | |
| α-helix | 510-532 | 23 | |
| α-helix | 535-536 | 2 | |
| α-helix | 538-563 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| α-helix | 30-39 | 10 | |
| α-helix | 46-53 | 8 | |
| α-helix | 66-74 | 9 | |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103-110 | 8 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-127 | 9 | |
| 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, B, D, G | protein | 692 | Homo sapiens | P51787 (AlphaFold model) |
| Calmodulin-3 | C, E, F, H | protein | 177 | Homo sapiens | P0DP25 (AlphaFold model) |
>7XNI_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, B, D, G) MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPG PAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGW KCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGC RSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLH VDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYA DALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQR QKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKK KKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFM RTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRD VIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVT QLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLP TYEQLTVPRRGPDEGSLEGGSSGGWSHPQFEK
>7XNI_2 Calmodulin-3 (chains C, E, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
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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