C-type inactivation in a voltage gated K+ channel. Determined by X-ray diffraction at 3.1 Å resolution. Released 4 May 2022.
Explore 7SIZ in 3D Show helices and sheets RCSB PDB PDBe
7SIZ contains 74 α-helices and 41 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 | 52-54 | 3 | 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 | 2 |
| β-strand | 218 | 1 | 4 |
| β-strand | 221 | 1 | 4 |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 247-252 | 6 | |
| α-helix | 271-277 | 7 | |
| 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 | 345-355 | 11 |
| 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 | 85-94 | 10 | |
| α-helix | 106-116 | 11 | |
| α-helix | 120-130 | 11 | |
| α-helix | 145-152 | 8 | |
| α-helix | 156-158 | 3 | |
| α-helix | 160-183 | 24 | |
| α-helix | 221-242 | 22 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-268 | 5 | |
| α-helix | 286-294 | 9 | |
| α-helix | 295-305 | 11 | |
| α-helix | 308-318 | 11 | |
| α-helix | 321-345 | 25 | |
| α-helix | 358-360 | 3 | |
| α-helix | 361-368 | 8 | |
| α-helix | 381-399 | 19 | |
| α-helix | 402-415 | 14 |
| 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 | 192-204 | 13 | |
| β-strand | 212-214 | 3 | 7 |
| β-strand | 216 | 1 | 9 |
| β-strand | 218 | 1 | 10 |
| β-strand | 221 | 1 | 10 |
| α-helix | 223 | 1 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| β-strand | 239-242 | 4 | 7 |
| β-strand | 243 | 1 | 9 |
| β-strand | 256 | 1 | 11 |
| β-strand | 258 | 1 | 11 |
| α-helix | 271-278 | 8 | |
| α-helix | 280-299 | 20 | |
| α-helix | 303-312 | 10 | |
| β-strand | 317-322 | 6 | 7 |
| α-helix | 327-334 | 8 | |
| α-helix | 336-342 | 7 | |
| α-helix | 345-355 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-39 | 6 | 12 |
| β-strand | 42-47 | 6 | 12 |
| α-helix | 48-51 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 12 |
| β-strand | 75-78 | 4 | 12 |
| α-helix | 85-94 | 10 | |
| α-helix | 106-116 | 11 | |
| α-helix | 119-130 | 12 | |
| α-helix | 145-149 | 5 | |
| α-helix | 160-182 | 23 | |
| α-helix | 221-243 | 23 | |
| α-helix | 254-261 | 8 | |
| α-helix | 286-295 | 10 | |
| α-helix | 296-305 | 10 | |
| α-helix | 308-318 | 11 | |
| α-helix | 321-345 | 25 | |
| α-helix | 361-368 | 8 | |
| α-helix | 381-399 | 19 | |
| α-helix | 402-415 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Voltage-gated potassium channel subunit beta-2 | A, C | protein | 333 | Rattus norvegicus | P62483 (AlphaFold model) |
| Voltage gated potassium channel Kv1.2-Kv2.1 | B, D | protein | 514 | Rattus norvegicus | P63142 (AlphaFold model) |
>7SIZ_1 Voltage-gated potassium channel subunit beta-2 (chains A, C) MLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGK AEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQ AEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI GAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
>7SIZ_2 Voltage gated potassium channel Kv1.2-Kv2.1 (chains B, D) MAHHHHHHHHHHGLVPRGSMTVATGDPVDEAAAHPGHPQDTYDPEADHESSERVVINISG LRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRP VNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGP ARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSQSTIGYQQSTSFTDP FFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYYVTIFLTESNKSVLQ FQNVRRVVQIFRIMRILRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSA VYFAEADERDSQFPSIPDAFFWAVVTMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALP VPVIVSNFNYFYHRETEGEEQAQYLQVTSSPKIPSSPDLKKSRSASTISKSDYMEIQEGV NNSNEDFREENLKTANSTLANTNYVNITKMLTDV
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 2 |
Water and common crystallization additives (K) are not listed.
Structural basis for C-type inactivation in a Shaker family voltage-gated K + channel. Reddi, R., Matulef, K., Riederer, E.A. et al. Sci Adv (2022) 8:eabm8804-eabm8804. DOI 10.1126/sciadv.abm8804 · PubMed
Other PDB entries of the same protein (UniProt P62483 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7SIZ 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.