Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Lys27Met mutant of Charybdotoxin. Determined by X-ray diffraction at 2.54 Å resolution. Released 12 Jun 2013.
Explore 4JTD in 3D Show helices and sheets RCSB PDB PDBe
4JTD contains 89 α-helices and 41 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.
| 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 | 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 | 133-147 | 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 | 4 |
| β-strand | 218 | 1 | 5 |
| β-strand | 221 | 1 | 5 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-236 | 8 | |
| β-strand | 239-242 | 4 | 2 |
| β-strand | 243 | 1 | 4 |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-39 | 6 | 6 |
| β-strand | 42-47 | 6 | 6 |
| α-helix | 48-51 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 6 |
| β-strand | 75-78 | 4 | 6 |
| α-helix | 82-93 | 12 | |
| α-helix | 99-101 | 3 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-129 | 10 | |
| α-helix | 146-149 | 4 | |
| α-helix | 161-182 | 22 | |
| α-helix | 186-189 | 4 | |
| α-helix | 202-210 | 9 | |
| α-helix | 221-242 | 22 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-274 | 11 | |
| α-helix | 279-283 | 5 | |
| α-helix | 286-294 | 9 | |
| α-helix | 295-306 | 12 | |
| α-helix | 308-318 | 11 | |
| α-helix | 321-345 | 25 | |
| α-helix | 357-368 | 12 | |
| α-helix | 381-399 | 19 | |
| α-helix | 402-414 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 39-41 | 3 | 7 |
| β-strand | 48-50 | 3 | 7 |
| β-strand | 52-55 | 4 | 8 |
| α-helix | 59-63 | 5 | |
| α-helix | 66-78 | 13 | |
| β-strand | 83-87 | 5 | 8 |
| α-helix | 90-93 | 4 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-112 | 3 | |
| β-strand | 114-119 | 6 | 8 |
| β-strand | 121 | 1 | 9 |
| α-helix | 126-128 | 3 | |
| β-strand | 129 | 1 | 9 |
| α-helix | 133-147 | 15 | |
| β-strand | 152-157 | 6 | 8 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 8 |
| α-helix | 192-205 | 14 | |
| α-helix | 208-210 | 3 | |
| β-strand | 212-216 | 5 | 8 |
| β-strand | 218 | 1 | 10 |
| β-strand | 221 | 1 | 10 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-236 | 8 | |
| β-strand | 239-243 | 5 | 8 |
| α-helix | 247-252 | 6 | |
| α-helix | 264-266 | 3 | |
| α-helix | 271-278 | 8 | |
| α-helix | 280-299 | 20 | |
| α-helix | 303-312 | 10 | |
| β-strand | 317-322 | 6 | 8 |
| α-helix | 327-334 | 8 | |
| α-helix | 336-339 | 4 | |
| α-helix | 345-355 | 11 | |
| α-helix | 358-360 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-39 | 6 | 11 |
| β-strand | 42-47 | 6 | 11 |
| α-helix | 48-51 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 11 |
| β-strand | 75-78 | 4 | 11 |
| α-helix | 82-94 | 13 | |
| α-helix | 99-101 | 3 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-130 | 11 | |
| α-helix | 164-167 | 4 | |
| α-helix | 169-183 | 15 | |
| α-helix | 221-239 | 19 | |
| α-helix | 250-252 | 3 | |
| α-helix | 254-260 | 7 | |
| α-helix | 264-268 | 5 | |
| α-helix | 279-281 | 3 | |
| α-helix | 290-294 | 5 | |
| α-helix | 295-306 | 12 | |
| α-helix | 308-318 | 11 | |
| α-helix | 321-345 | 25 | |
| α-helix | 357-368 | 12 | |
| α-helix | 381-398 | 18 | |
| α-helix | 401-415 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 12 |
| α-helix | 10-16 | 7 | |
| β-strand | 26-27 | 2 | 12 |
| β-strand | 34-35 | 2 | 12 |
| 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) |
>4JTD_1 Voltage-gated potassium channel subunit beta-2 (chains A, G) MLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGK AEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQ AEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI GAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
>4JTD_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
>4JTD_3 Potassium channel toxin alpha-KTx 1.1 (chains Y) QFTNVSCTTSKECWSVCQRLHNTSRGMCMNKKCRCYS
| ID | Name | Formula | Copies |
|---|---|---|---|
| PGW | (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade… | C40 H77 O10 P | 17 |
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 2 |
Water and common crystallization additives (K) are not listed.
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:
MolViewer shows 4JTD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.