XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2. Determined by electron microscopy at 2.5 Å resolution. Released 3 Jun 2026.
Explore 22BF in 3D Show helices and sheets RCSB PDB PDBe
22BF contains 57 α-helices and 4 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 | 104-116 | 13 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-143 | 21 | |
| α-helix | 149-176 | 28 | |
| α-helix | 177-180 | 4 | |
| α-helix | 187-192 | 6 | |
| α-helix | 193-195 | 3 | |
| α-helix | 197-209 | 13 | |
| α-helix | 231-236 | 6 | |
| α-helix | 237-240 | 4 | |
| α-helix | 245-256 | 12 | |
| α-helix | 258-281 | 24 | |
| α-helix | 303-314 | 12 | |
| α-helix | 327-344 | 18 | |
| α-helix | 346-365 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-86 | 15 | |
| α-helix | 93-113 | 21 | |
| α-helix | 120-147 | 28 | |
| α-helix | 148-150 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-209 | 14 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| β-strand | 255 | 1 | 1 |
| β-strand | 258 | 1 | 1 |
| α-helix | 264-275 | 12 | |
| α-helix | 288-305 | 18 | |
| α-helix | 307-326 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-85 | 14 | |
| α-helix | 90-92 | 3 | |
| α-helix | 93-114 | 22 | |
| α-helix | 119-147 | 29 | |
| α-helix | 148-150 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 196-198 | 3 | |
| α-helix | 201-204 | 4 | |
| α-helix | 205-210 | 6 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| α-helix | 264-275 | 12 | |
| α-helix | 288-326 | 39 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-85 | 14 | |
| α-helix | 90-92 | 3 | |
| α-helix | 93-112 | 20 | |
| α-helix | 116-147 | 32 | |
| α-helix | 148-150 | 3 | |
| α-helix | 152-154 | 3 | |
| α-helix | 156-164 | 9 | |
| α-helix | 167-183 | 17 | |
| α-helix | 198-204 | 7 | |
| α-helix | 205-210 | 6 | |
| α-helix | 213-215 | 3 | |
| α-helix | 216-227 | 12 | |
| α-helix | 229-254 | 26 | |
| β-strand | 255 | 1 | 2 |
| β-strand | 258 | 1 | 2 |
| α-helix | 264-275 | 12 | |
| α-helix | 288-305 | 18 | |
| α-helix | 307-326 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 3 | A | protein | 872 | Homo sapiens | O43525 (AlphaFold model) |
| Potassium voltage-gated channel subfamily KQT member 2 | B, C, D | protein | 872 | Homo sapiens | O43526 (AlphaFold model) |
>22BF_1 Potassium voltage-gated channel subfamily KQT member 3 (chains A) MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAG ADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRG WALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGC CCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRM DRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEF ETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQ EQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAAS SQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKA YAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRP YDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPR NEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPT KGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNL PRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRR SITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDT DTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
>22BF_2 Potassium voltage-gated channel subfamily KQT member 2 (chains B, C, D) MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAG GAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEK SSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGF LCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLI GVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSP CRGPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKV PKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSI RAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAIT DKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFG AKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQP QSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGN LRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESD TDSDLCTPCGPPPRSATGEGPFGDVGWAGPRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1EY8 | Azetukalner | C23 H29 F N2 O | 4 |
Water and common crystallization additives (K) are not listed.
Structural basis for the assembly and modulation of human M-channels. Lu, F., Huang, X., Cai, G. et al. To be published.
Other PDB entries of the same protein (UniProt O43525 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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