22RQ: PDB entry 22RQ

Human KCNQ3-XEN1101 complex in the presence of PIP2. Determined by electron microscopy at 2.9 Å resolution. Released 3 Jun 2026.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,260
Mol. weight: 388.94 kDa
Ligands: A1EY8
Released: 3 Jun 2026

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

Secondary structure: helices and β-sheets

22RQ 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.

Chains A, B, C and D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	106-115	10
α-helix	120-122	3
α-helix	123-143	21
α-helix	149-180	32
α-helix	187-193	7
α-helix	197-208	12
α-helix	210-213	4
α-helix	227-237	11
α-helix	245-256	12
α-helix	260-283	24
α-helix	303-314	12
α-helix	327-340	14
α-helix	342-376	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily KQT member 3	A, B, C, D	protein	872	Homo sapiens	O43525 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>22RQ_1 Potassium voltage-gated channel subfamily KQT member 3 (chains A, B, C, D)
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAG
ADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRG
WALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGC
CCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRM
DRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEF
ETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQ
EQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAAS
SQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKA
YAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRP
YDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPR
NEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPT
KGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNL
PRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRR
SITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDT
DTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI

Ligands and cofactors

ID	Name	Formula	Copies
A1EY8	Azetukalner	C23 H29 F N2 O	4

Primary citation

Human KCNQ3-XEN1101 complex in the presence of PIP2. Cheng, X.Y., Wan, S.Y., Jiang, D.X. 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:

5J03 2.0 Å, Crystal Structure of a chimeric Kv7.2 - Kv7.3 proximal C-terminal Domain in Complex with…
22BJ 2.4 Å, KCNQ2/3 heterotetramer with 3:1 stoichiometry
22BF 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2
22BG 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
22BE 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
22BI 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 2:2 stoichiometry
22AZ 2.7 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
22BK 2.7 Å, KCNQ2/3 heterotetramer with 2:2 stoichiometry
22BC 2.8 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
22BH 2.8 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 4
22RJ 2.82 Å, Human KCNQ3-CaM in apo state
22BA 2.9 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2

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