8VC3: Voltage gated potassium ion channel Kv1.2

Voltage gated potassium ion channel Kv1.2 in complex with DTx. Determined by electron microscopy at 3.2 Å resolution. Released 10 Jul 2024.

Method
Electron microscopy
Resolution
3.2 Å
Organisms
Dendroaspis angusticeps, Rattus norvegicus
Chains
5
Atoms
8,219
Mol. weight
249.46 kDa
Released
10 Jul 2024

Explore 8VC3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VC3 contains 56 α-helices and 3 β-strands across 5 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.

Chain A: 1 helix, 3 β-strands

ElementResiduesLengthSheet
β-strand20-2671
β-strand31-3771
β-strand4711
α-helix50-556
Chain B: 14 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix146-1549
α-helix156-1583
α-helix160-18223
α-helix186-1905
α-helix221-24323
α-helix250-2523
α-helix254-27320
α-helix291-2988
α-helix299-30911
α-helix312-32312
α-helix325-34925
α-helix361-37212
α-helix385-40319
α-helix406-41813
Chain C: 14 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix146-1549
α-helix156-1583
α-helix160-18223
α-helix186-1905
α-helix221-24222
α-helix250-2523
α-helix254-27320
α-helix291-2999
α-helix300-3089
α-helix312-32312
α-helix325-34925
α-helix361-37212
α-helix385-40319
α-helix406-41813
Chain D: 14 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix146-1549
α-helix156-1583
α-helix160-18324
α-helix186-1905
α-helix221-24323
α-helix250-2523
α-helix254-27320
α-helix291-2999
α-helix300-3089
α-helix312-32312
α-helix325-34925
α-helix361-37212
α-helix385-40319
α-helix406-41813
Chain E: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix146-1549
α-helix156-1583
α-helix160-18223
α-helix186-1894
α-helix221-24222
α-helix254-27320
α-helix291-2999
α-helix300-30910
α-helix312-32312
α-helix325-34925
α-helix361-37212
α-helix385-40319
α-helix406-41813

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kunitz-type serine protease inhibitor homolog alpha-dendrotoxinAprotein59Dendroaspis angusticepsP00980 (AlphaFold model)
Potassium voltage-gated channel subfamily A member 2B, C, D, Eprotein536Rattus norvegicusP63142 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8VC3_1 Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin (chains A)
GPRRKLCILHRNPGRCYDKIPAFYYNQKKKQCERFDWSGCGGNSNRFKTIEECRRTCIG
Sequence of entity 2 (B, C, D, E), FASTA
>8VC3_2 Potassium voltage-gated channel subfamily A member 2 (chains B, C, D, E)
MSAWSHPQFEKGGGSGGGSGGSAWSHPQFEKLVPRGSMTVATGDPVDEAAAHPGHPQDTY
DPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRP
SFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPEN
EFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGSGVTFH
TYSQSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAI
IPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKA
SMRELGLLIFFLFIGVILFSSAVYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPT
TIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPD
LKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV

Primary citation

Cryo-EM structures of Kv1.2 potassium channels, conducting and non-conducting. Wu, Y., Yan, Y., Yang, Y. et al. bioRxiv (2024). DOI 10.1101/2023.06.02.543446 · PubMed

Other PDB entries of the same protein (UniProt P00980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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