9VEI: Human KCNQ1-KCNE1-CaM complex with PIP2

structure of human KCNQ1-KCNE1-CaM complex with PIP2. Determined by electron microscopy at 3.9 Å resolution. Released 20 Aug 2025.

Method
Electron microscopy
Resolution
3.9 Å
Organism
Homo sapiens
Chains
12
Atoms
15,940
Mol. weight
383.07 kDa
Ligands
CA, PT5
Released
20 Aug 2025

Explore 9VEI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VEI contains 120 α-helices and 8 β-strands across 12 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.

Chains A, D, G and J: 19 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix105-11410
α-helix119-14527
α-helix149-1513
α-helix155-17622
α-helix177-1793
α-helix182-1843
α-helix186-1938
α-helix197-21620
α-helix226-23712
α-helix238-2414
α-helix246-25712
α-helix259-28426
α-helix299-31012
α-helix323-33614
α-helix338-3403
α-helix342-38241
α-helix507-53327
α-helix552-5609
α-helix588-61932
Chains B, E, H and K: 8 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix10-189
α-helix30-4011
α-helix46-5611
α-helix69-735
α-helix80-9112
β-strand101-10221
α-helix103-11210
α-helix119-12911
β-strand136-13721
α-helix139-1468
Chains C, F, I and L: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix42-6726
α-helix69-702
α-helix76-794

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Potassium voltage-gated channel subfamily KQT member 1A, D, G, Jprotein546Homo sapiensP51787 (AlphaFold model)
Calmodulin-1B, E, H, Kprotein149Homo sapiensP0DP23 (AlphaFold model)
Potassium voltage-gated channel subfamily E member 1C, F, I, Lprotein129Homo sapiensP15382 (AlphaFold model)
Sequence of entity 1 (A, D, G, J), FASTA
>9VEI_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, D, G, J)
MASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVL
VCLIFSVLSTCEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFA
RKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSV
VFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIG
YGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASL
IQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPG
EKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGE
TLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMV
RIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLH
QLLSLH
Sequence of entity 2 (B, E, H, K), FASTA
>9VEI_2 Calmodulin-1 (chains B, E, H, K)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK
Sequence of entity 3 (C, F, I, L), FASTA
>9VEI_3 Potassium voltage-gated channel subfamily E member 1 (chains C, F, I, L)
MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGCLEALYVLMVLGFFGFFTLG
IMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNT
HLPETKPSP

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa8
PT5[(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4…C47 H85 O19 P38

Primary citation

Mechanisms of KCNQ1 gating modulation by KCNE1/3 for cell-specific function. Cui, C., Zhao, L., Kermani, A.A. et al. Cell Res (2025) 35:876-886. DOI 10.1038/s41422-025-01152-1 · PubMed

Other PDB entries of the same protein (UniProt P51787 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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