8VC6: PDB entry 8VC6

Voltage gated potassium ion channel Kv1.2 in Potassium. Determined by electron microscopy at 3.17 Å resolution. Released 10 Jul 2024.

Method: Electron microscopy
Resolution: 3.17 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 7,740
Mol. weight: 242.37 kDa
Released: 10 Jul 2024

Explore 8VC6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VC6 contains 55 α-helices and 0 β-strands across 4 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	146-154	9
α-helix	156-158	3
α-helix	160-183	24
α-helix	186-189	4
α-helix	221-241	21
α-helix	248-252	5
α-helix	254-273	20
α-helix	291-299	9
α-helix	300-309	10
α-helix	312-323	12
α-helix	325-349	25
α-helix	361-372	12
α-helix	385-402	18
α-helix	406-418	13

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	146-154	9
α-helix	156-158	3
α-helix	160-183	24
α-helix	186-189	4
α-helix	221-241	21
α-helix	248-251	4
α-helix	254-273	20
α-helix	291-299	9
α-helix	300-309	10
α-helix	312-323	12
α-helix	325-349	25
α-helix	361-372	12
α-helix	385-402	18
α-helix	406-418	13

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	146-154	9
α-helix	160-183	24
α-helix	186-189	4
α-helix	221-242	22
α-helix	250-252	3
α-helix	254-273	20
α-helix	291-299	9
α-helix	300-309	10
α-helix	312-323	12
α-helix	325-349	25
α-helix	361-372	12
α-helix	385-402	18
α-helix	406-418	13

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	146-154	9
α-helix	156-158	3
α-helix	160-183	24
α-helix	186-189	4
α-helix	221-241	21
α-helix	247-252	6
α-helix	254-273	20
α-helix	291-299	9
α-helix	300-309	10
α-helix	312-323	12
α-helix	325-349	25
α-helix	361-372	12
α-helix	385-402	18
α-helix	406-418	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily A member 2	A, B, C, D	protein	536	Rattus norvegicus	P63142 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8VC6_1 Potassium voltage-gated channel subfamily A member 2 (chains A, B, C, D)
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 P63142 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DSX 1.6 Å, KV1.2 T1 domain, residues 33-119, T46V mutant
1QDV 1.6 Å, N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-131
1QDW 2.1 Å, N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-119
4JTA 2.5 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin
4JTD 2.54 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Lys27Met mutant of…
8VCH 2.55 Å, Voltage gated potassium ion channel Kv1.2 W366F, C-type inactivated
4JTC 2.56 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+
2A79 2.9 Å, Mammalian Shaker Kv1.2 potassium channel- beta subunit complex
3LNM 2.9 Å, F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel
3LUT 2.9 Å, A Structural Model for the Full-length Shaker Potassium Channel Kv1.2
6EBL 3.0 Å, The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic…
7SIZ 3.1 Å, C-type inactivation in a voltage gated K+ channel

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