Shaker family voltage dependent potassium channel (kv1.2-kv2.1 paddle chimera channel) in association with beta subunit. Determined by X-ray diffraction at 2.4 Å resolution. Released 20 Nov 2007.
Explore 2R9R in 3D Show helices and sheets RCSB PDB PDBe
2R9R contains 88 α-helices and 38 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 |
|---|---|---|---|
| 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 | 83-85 | 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 | 133-147 | 15 | |
| β-strand | 152-157 | 6 | 2 |
| α-helix | 166-178 | 13 | |
| β-strand | 182-188 | 7 | 2 |
| α-helix | 192-204 | 13 | |
| 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 | 280-298 | 19 | |
| α-helix | 303-311 | 9 | |
| β-strand | 317-322 | 6 | 2 |
| α-helix | 327-334 | 8 | |
| 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 | 82-94 | 13 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-129 | 10 | |
| α-helix | 146-151 | 6 | |
| α-helix | 160-182 | 23 | |
| α-helix | 186-189 | 4 | |
| α-helix | 202-210 | 9 | |
| α-helix | 221-243 | 23 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-274 | 11 | |
| α-helix | 279-283 | 5 | |
| α-helix | 286-295 | 10 | |
| α-helix | 296-305 | 10 | |
| α-helix | 308-319 | 12 | |
| α-helix | 321-346 | 26 | |
| α-helix | 357-368 | 12 | |
| α-helix | 381-399 | 19 | |
| α-helix | 402-416 | 15 |
| 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 | 83-85 | 3 | 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 | 303-311 | 9 | |
| β-strand | 317-322 | 6 | 8 |
| α-helix | 327-334 | 8 | |
| 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 | 11 |
| β-strand | 42-47 | 6 | 11 |
| α-helix | 48-52 | 5 | |
| 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 | 106-115 | 10 | |
| α-helix | 120-129 | 10 | |
| α-helix | 146-151 | 6 | |
| α-helix | 160-182 | 23 | |
| α-helix | 186-189 | 4 | |
| α-helix | 203-210 | 8 | |
| α-helix | 221-243 | 23 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-274 | 11 | |
| α-helix | 279-283 | 5 | |
| α-helix | 286-295 | 10 | |
| α-helix | 296-305 | 10 | |
| α-helix | 308-319 | 12 | |
| α-helix | 321-346 | 26 | |
| α-helix | 357-368 | 12 | |
| α-helix | 381-399 | 19 | |
| α-helix | 402-416 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Voltage-gated potassium channel subunit beta-2 | A, G | protein | 333 | Rattus norvegicus | P62483 (AlphaFold model) |
| Paddle chimera voltage gated potassium channel Kv1.2-Kv2.1 | B, H | protein | 514 | Rattus norvegicus |
>2R9R_1 Voltage-gated potassium channel subunit beta-2 (chains A, G) MLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGK AEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQ AEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI GAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
>2R9R_2 Paddle chimera voltage gated potassium channel Kv1.2-Kv2.1 (chains B, H) MAHHHHHHHHHHGLVPRGSMTVATGDPVDEAAALPGHPQDTYDPEADHESSERVVINISG LRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRP VNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGP ARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSQSTIGYQQSTSFTDP FFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYYVTIFLTESNKSVLQ FQNVRRVVQIFRIMRILRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSA VYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALP VPVIVSNFNYFYHRETEGEEQAQYLQVTSSPKIPSSPDLKKSRSASTISKSDYMEIQEGV NNSNEDFREENLKTANSTLANTNYVNITKMLTDV
| 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.
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Long, S.B., Tao, X., Campbell, E.B. et al. Nature (2007) 450:376-382. DOI 10.1038/nature06265 · PubMed
Other PDB entries of the same protein (UniProt P62483 (AlphaFold model), which also has an AlphaFold model), best resolution first:
2R9R is part of these collections:
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