22BG: PDB entry 22BG

XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3. Determined by electron microscopy at 2.5 Å resolution. Released 3 Jun 2026.

Method
Electron microscopy
Resolution
2.5 Å
Organism
Homo sapiens
Chains
4
Atoms
8,139
Mol. weight
386.39 kDa
Ligands
A1EY8
Released
3 Jun 2026

Explore 22BG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

22BG contains 52 α-helices and 0 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.

Chain A: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix104-11613
α-helix121-14323
α-helix149-17628
α-helix177-1804
α-helix187-1926
α-helix193-1953
α-helix197-20913
α-helix232-2387
α-helix245-25612
α-helix258-28124
α-helix303-31412
α-helix327-36539
Chain B: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix72-8615
α-helix92-11423
α-helix119-14729
α-helix148-1503
α-helix152-1543
α-helix156-1649
α-helix167-18317
α-helix197-20913
α-helix213-2153
α-helix216-22712
α-helix229-25426
α-helix264-27512
α-helix288-32639
Chain C: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix72-8615
α-helix92-11322
α-helix119-14729
α-helix148-1503
α-helix152-1543
α-helix156-1649
α-helix167-18317
α-helix197-20913
α-helix213-2153
α-helix216-22712
α-helix229-25426
α-helix264-27512
α-helix288-32639
Chain D: 14 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix72-8615
α-helix90-923
α-helix93-11220
α-helix119-14729
α-helix148-1503
α-helix156-1649
α-helix167-18317
α-helix196-1983
α-helix203-2108
α-helix213-2153
α-helix216-22712
α-helix229-25426
α-helix264-27512
α-helix288-32639

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Potassium voltage-gated channel subfamily KQT member 3Aprotein872Homo sapiensO43525 (AlphaFold model)
Potassium voltage-gated channel subfamily KQT member 2B, C, Dprotein872Homo sapiensO43526 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>22BG_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
Sequence of entity 2 (B, C, D), FASTA
>22BG_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

Ligands and cofactors

IDNameFormulaCopies
A1EY8AzetukalnerC23 H29 F N2 O4

Water and common crystallization additives (K) are not listed.

Primary citation

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:

Browse structure collections

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