4JTC: Kv1.2-2.1 paddle chimera channel
Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+. Determined by X-ray diffraction at 2.56 Å resolution. Released 12 Jun 2013.
- Method
- X-ray diffraction
- Resolution
- 2.56 Å
- Organisms
- Rattus norvegicus, Leiurus quinquestriatus hebraeus
- Chains
- 5
- Atoms
- 11,770
- Mol. weight
- 211.94 kDa
- Ligands
- PGW, CS, NAP
- Released
- 12 Jun 2013
Explore 4JTC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4JTC contains 89 α-helices and 39 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: 22 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 | 66-78 | 13 | |
| β-strand | 83-87 | 5 | 2 |
| 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 | 133-147 | 15 | |
| β-strand | 152-157 | 6 | 2 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 2 |
| α-helix | 192-205 | 14 | |
| α-helix | 208-210 | 3 | |
| 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 | 229-236 | 8 | |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 247-252 | 6 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-299 | 20 | |
| α-helix | 303-311 | 9 | |
| β-strand | 317-322 | 6 | 2 |
| α-helix | 327-333 | 7 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-342 | 3 | |
| α-helix | 345-355 | 11 | |
| α-helix | 358-360 | 3 | |
Chain B: 22 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 | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 5 |
| β-strand | 75-78 | 4 | 5 |
| α-helix | 82-94 | 13 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-129 | 10 | |
| α-helix | 146-149 | 4 | |
| α-helix | 160-182 | 23 | |
| α-helix | 186-189 | 4 | |
| α-helix | 202-210 | 9 | |
| α-helix | 221-242 | 22 | |
| α-helix | 247-252 | 6 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-275 | 12 | |
| α-helix | 279-282 | 4 | |
| α-helix | 286-294 | 9 | |
| α-helix | 295-305 | 11 | |
| α-helix | 308-319 | 12 | |
| α-helix | 321-345 | 25 | |
| α-helix | 357-368 | 12 | |
| α-helix | 381-399 | 19 | |
| α-helix | 401-414 | 14 | |
Chain G: 22 helices, 14 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 | 66-78 | 13 | |
| β-strand | 83-87 | 5 | 7 |
| α-helix | 90-93 | 4 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-112 | 3 | |
| β-strand | 114-119 | 6 | 7 |
| β-strand | 121 | 1 | 8 |
| α-helix | 126-128 | 3 | |
| β-strand | 129 | 1 | 8 |
| α-helix | 133-147 | 15 | |
| β-strand | 152-157 | 6 | 7 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 7 |
| α-helix | 192-205 | 14 | |
| α-helix | 208-210 | 3 | |
| β-strand | 212-216 | 5 | 7 |
| β-strand | 218 | 1 | 9 |
| β-strand | 221 | 1 | 9 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-236 | 8 | |
| β-strand | 239-243 | 5 | 7 |
| α-helix | 247-252 | 6 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-299 | 20 | |
| α-helix | 303-311 | 9 | |
| β-strand | 317-322 | 6 | 7 |
| α-helix | 327-334 | 8 | |
| α-helix | 336-339 | 4 | |
| α-helix | 345-355 | 11 | |
| α-helix | 358-360 | 3 | |
Chain H: 21 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 10 |
| β-strand | 42-47 | 6 | 10 |
| α-helix | 48-51 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 10 |
| β-strand | 75-78 | 4 | 10 |
| α-helix | 82-94 | 13 | |
| α-helix | 99-101 | 3 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-128 | 9 | |
| α-helix | 151-154 | 4 | |
| α-helix | 160-181 | 22 | |
| α-helix | 221-237 | 17 | |
| α-helix | 248-250 | 3 | |
| α-helix | 254-256 | 3 | |
| α-helix | 257-260 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 287-290 | 4 | |
| α-helix | 296-302 | 7 | |
| α-helix | 308-318 | 11 | |
| α-helix | 323-345 | 23 | |
| α-helix | 357-368 | 12 | |
| α-helix | 383-397 | 15 | |
| α-helix | 401-413 | 13 | |
Chain Y: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-12 | 3 | |
| α-helix | 14-20 | 7 | |
| β-strand | 28 | 1 | 11 |
| β-strand | 33 | 1 | 11 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Voltage-gated potassium channel subunit beta-2 | A, G | protein | 333 | Rattus norvegicus | P62483 (AlphaFold model) |
| Potassium voltage-gated channel subfamily A member 2, Potassium voltage-gated channel subfamily B… | B, H | protein | 514 | Rattus norvegicus | P15387 (AlphaFold model), P63142 (AlphaFold model) |
| Potassium channel toxin alpha-KTx 1.1 | Y | protein | 37 | Leiurus quinquestriatus hebraeus | P13487 (AlphaFold model) |
Sequence of entity 1 (A, G), FASTA
>4JTC_1 Voltage-gated potassium channel subunit beta-2 (chains A, G)
MLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGK
AEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV
VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQ
AEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK
DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI
GAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
Sequence of entity 2 (B, H), FASTA
>4JTC_2 Potassium voltage-gated channel subfamily A member 2, Potassium voltage-gated channel subfamily B member 1 (chains B, H)
MAHHHHHHHHHHGLVPRGSMTVATGDPVDEAAALPGHPQDTYDPEADHESSERVVINISG
LRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRP
VNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGP
ARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSQSTIGYQQSTSFTDP
FFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYYVTIFLTESNKSVLQ
FQNVRRVVQIFRIMRILRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSA
VYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALP
VPVIVSNFNYFYHRETEGEEQAQYLQVTSSPKIPSSPDLKKSRSASTISKSDYMEIQEGV
NNSNEDFREENLKTANSTLANTNYVNITKMLTDV
Sequence of entity 3 (Y), FASTA
>4JTC_3 Potassium channel toxin alpha-KTx 1.1 (chains Y)
QFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PGW | (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade… | C40 H77 O10 P | 17 |
| CS | Cesium ion | Cs | 8 |
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 2 |
Primary citation
Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel. Banerjee, A., Lee, A., Campbell, E. et al. Elife (2013) 2:e00594-e00594. DOI 10.7554/eLife.00594 · 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…
- 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
- 6EBL 3.0 Å, The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic…
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