The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha. Determined by electron microscopy at 4.0 Å resolution. Released 22 Aug 2018.
Explore 6EBM in 3D Show helices and sheets RCSB PDB PDBe
6EBM contains 63 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 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) |
>6EBM_1 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
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 P63142 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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