6EBK: Voltage-gated potassium channel subunit beta-2
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs. Determined by electron microscopy at 3.3 Å resolution. Released 22 Aug 2018.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organism
- Rattus norvegicus
- Chains
- 8
- Atoms
- 22,212
- Mol. weight
- 387.95 kDa
- Ligands
- NAP
- Released
- 22 Aug 2018
Explore 6EBK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6EBK contains 155 α-helices and 76 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.
Chain A: 19 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-41 | 3 | 1 |
| β-strand | 48-50 | 3 | 1 |
| β-strand | 52-55 | 4 | 2 |
| α-helix | 59-63 | 5 | |
| α-helix | 66-77 | 12 | |
| β-strand | 83-85 | 3 | 2 |
| α-helix | 90-93 | 4 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-112 | 3 | |
| β-strand | 114-119 | 6 | 2 |
| β-strand | 121 | 1 | 3 |
| α-helix | 126-128 | 3 | |
| β-strand | 129 | 1 | 3 |
| α-helix | 133-146 | 14 | |
| β-strand | 152-157 | 6 | 2 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 2 |
| α-helix | 192-204 | 13 | |
| β-strand | 212-214 | 3 | 2 |
| β-strand | 216 | 1 | 2 |
| β-strand | 218 | 1 | 4 |
| β-strand | 221 | 1 | 4 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| β-strand | 240-243 | 4 | 2 |
| α-helix | 254-257 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-298 | 19 | |
| α-helix | 303-309 | 7 | |
| β-strand | 317-322 | 6 | 2 |
| α-helix | 327-334 | 8 | |
| α-helix | 345-355 | 11 | |
Chains B, D and H: 20 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 5 |
| β-strand | 42-47 | 6 | 5 |
| α-helix | 48-51 | 4 | |
| α-helix | 65-68 | 4 | |
| β-strand | 69-70 | 2 | 5 |
| β-strand | 75-78 | 4 | 5 |
| α-helix | 85-94 | 10 | |
| α-helix | 106-113 | 8 | |
| α-helix | 121-130 | 10 | |
| α-helix | 146-152 | 7 | |
| α-helix | 160-183 | 24 | |
| α-helix | 204-205 | 2 | |
| α-helix | 206-210 | 5 | |
| α-helix | 221-242 | 22 | |
| α-helix | 248-251 | 4 | |
| α-helix | 254-275 | 22 | |
| α-helix | 287-295 | 9 | |
| α-helix | 296-305 | 10 | |
| α-helix | 308-318 | 11 | |
| α-helix | 324-345 | 22 | |
| α-helix | 360-368 | 9 | |
| α-helix | 381-398 | 18 | |
| α-helix | 402-413 | 12 | |
| α-helix | 414-416 | 3 | |
Chains C and E: 19 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-41 | 3 | 6 |
| β-strand | 48-50 | 3 | 6 |
| β-strand | 52-55 | 4 | 7 |
| α-helix | 59-63 | 5 | |
| α-helix | 66-77 | 12 | |
| β-strand | 83-85 | 3 | 7 |
| α-helix | 90-93 | 4 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 7 |
| β-strand | 121 | 1 | 8 |
| α-helix | 126-128 | 3 | |
| β-strand | 129 | 1 | 8 |
| α-helix | 133-146 | 14 | |
| β-strand | 152-157 | 6 | 7 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 7 |
| α-helix | 192-204 | 13 | |
| β-strand | 212-214 | 3 | 7 |
| β-strand | 216 | 1 | 7 |
| β-strand | 218 | 1 | 9 |
| β-strand | 221 | 1 | 9 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| β-strand | 240-243 | 4 | 7 |
| α-helix | 254-257 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-298 | 19 | |
| α-helix | 303-309 | 7 | |
| β-strand | 317-322 | 6 | 7 |
| α-helix | 327-334 | 8 | |
| α-helix | 345-355 | 11 | |
Chain F: 19 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 15 |
| β-strand | 42-47 | 6 | 15 |
| α-helix | 48-51 | 4 | |
| α-helix | 65-68 | 4 | |
| β-strand | 69-70 | 2 | 15 |
| β-strand | 75-78 | 4 | 15 |
| α-helix | 85-94 | 10 | |
| α-helix | 106-113 | 8 | |
| α-helix | 121-130 | 10 | |
| α-helix | 146-152 | 7 | |
| α-helix | 160-183 | 24 | |
| α-helix | 204-209 | 6 | |
| α-helix | 221-242 | 22 | |
| α-helix | 248-251 | 4 | |
| α-helix | 254-274 | 21 | |
| α-helix | 287-295 | 9 | |
| α-helix | 296-305 | 10 | |
| α-helix | 308-318 | 11 | |
| α-helix | 323-345 | 23 | |
| α-helix | 360-368 | 9 | |
| α-helix | 381-398 | 18 | |
| α-helix | 402-413 | 12 | |
| α-helix | 414-416 | 3 | |
Chain G: 19 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-41 | 3 | 16 |
| β-strand | 48-50 | 3 | 16 |
| β-strand | 52-55 | 4 | 17 |
| α-helix | 59-63 | 5 | |
| α-helix | 66-77 | 12 | |
| β-strand | 83-85 | 3 | 17 |
| α-helix | 90-93 | 4 | |
| α-helix | 94-105 | 12 | |
| α-helix | 110-112 | 3 | |
| β-strand | 114-118 | 5 | 17 |
| β-strand | 121 | 1 | 18 |
| α-helix | 126-128 | 3 | |
| β-strand | 129 | 1 | 18 |
| α-helix | 133-146 | 14 | |
| β-strand | 152-157 | 6 | 17 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 17 |
| α-helix | 192-204 | 13 | |
| β-strand | 212-214 | 3 | 17 |
| β-strand | 216 | 1 | 17 |
| β-strand | 218 | 1 | 19 |
| β-strand | 221 | 1 | 19 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| β-strand | 240-243 | 4 | 17 |
| α-helix | 254-257 | 4 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-298 | 19 | |
| α-helix | 303-309 | 7 | |
| β-strand | 317-322 | 6 | 17 |
| α-helix | 327-334 | 8 | |
| α-helix | 345-355 | 11 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Voltage-gated potassium channel subunit beta-2 | A, C, E, G | protein | 333 | Rattus norvegicus | P62483 (AlphaFold model) |
| Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B… | B, D, F, H | protein | 513 | Rattus norvegicus | P63142 (AlphaFold model), Q63099 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>6EBK_1 Voltage-gated potassium channel subunit beta-2 (chains A, C, E, G)
MVQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGK
AEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV
VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQ
AEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK
DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI
GAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
Sequence of entity 2 (B, D, F, H), FASTA
>6EBK_2 Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera (chains B, D, F, H)
MAHHHHHHHHENLYFQGSMTVATGDPVDEAAAHPGHPQDTYDPEADHECCERVVINISGL
RFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPV
NVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPA
RIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSQSTIGYQQSTSFTDPF
FIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYYVTIFLTESNKSVLQF
QNVRRVVQIFRIMRILRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAV
YFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPV
PVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVN
NSNEDFREENLKTANCTLANTNYVNITKMLTDV
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 4 |
Primary citation
Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs. Matthies, D., Bae, C., Toombes, G.E. et al. Elife (2018) 7. DOI 10.7554/eLife.37558 · PubMed
Other PDB entries of the same protein (UniProt P62483 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3EAU 1.82 Å, Voltage-dependent K+ channel beta subunit in complex with cortisone
- 3EB3 2.0 Å, Voltage-dependent K+ channel beta subunit (W121A) in complex with cortisone
- 3EB4 2.0 Å, Voltage-dependent K+ channel beta subunit (I211R) in complex with cortisone
- 1EXB 2.1 Å, Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K channels
- 2R9R 2.4 Å, Shaker family voltage dependent potassium channel (kv1.2-kv2.1 paddle chimera channel)…
- 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…
- 4JTC 2.56 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+
- 1QRQ 2.8 Å, Structure of a voltage-dependent K+ channel beta subunit
- 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
Browse structure collections
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