7VNR: Human KCNQ4-ML213 complex in digitonin

Structure of human KCNQ4-ML213 complex in digitonin. Determined by electron microscopy at 2.8 Å resolution. Released 1 Dec 2021.

Method: Electron microscopy
Resolution: 2.8 Å
Organisms: Homo sapiens, Escherichia coli (strain B / BL21-DE3)
Chains: 8
Atoms: 15,343
Mol. weight: 534.72 kDa
Ligands: 7YV
Released: 1 Dec 2021

Explore 7VNR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7VNR contains 88 α-helices and 16 β-strands across 8 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	75-92	18
α-helix	100-118	19
α-helix	127-153	27
α-helix	163-169	7
α-helix	176-189	14
α-helix	200-215	16
α-helix	222-233	12
α-helix	235-260	26
α-helix	270-281	12
α-helix	294-333	40
α-helix	340-354	15
α-helix	533-551	19
α-helix	558-585	28

Chains B, D, F and H: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-19	12
β-strand	26-27	2	1
α-helix	29-38	10
α-helix	45-53	9
β-strand	63-64	2	1
α-helix	65-74	10
α-helix	79-91	13
β-strand	99-101	3	2
α-helix	102-111	10
α-helix	115-117	3
α-helix	118-127	10
β-strand	135-137	3	2
α-helix	138-145	8

Chains C and G: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	75-92	18
α-helix	100-118	19
α-helix	127-153	27
α-helix	163-169	7
α-helix	176-189	14
α-helix	200-215	16
α-helix	222-233	12
α-helix	235-260	26
α-helix	270-281	12
α-helix	294-333	40
α-helix	340-354	15
α-helix	533-553	21
α-helix	558-585	28

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	75-92	18
α-helix	100-118	19
α-helix	127-153	27
α-helix	163-169	7
α-helix	176-189	14
α-helix	200-215	16
α-helix	222-233	12
α-helix	235-260	26
α-helix	270-281	12
α-helix	294-334	41
α-helix	340-354	15
α-helix	533-553	21
α-helix	558-585	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily KQT member 4,Maltodextrin-binding protein	A, C, E, G	protein	1049	Homo sapiens, Escherichia coli (strain B / BL21-DE3)	P56696 (AlphaFold model)
Calmodulin-3	B, D, F, H	protein	149	Homo sapiens	P0DP25 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>7VNR_1 Potassium voltage-gated channel subfamily KQT member 4,Maltodextrin-binding protein (chains A, C, E, G)
MDYKDDDDKAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPL
PPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSC
LVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARK
PFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVY
AHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPH
TWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRL
YSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRY
PPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGE
ATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKT
VIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPG
DRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSALE
VLFQGPMAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAA
TGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEA
LSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYE
NGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAW
SNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEA
VNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAAS
GRQTVDEALKDAQTNAAAEHHHHHHHHHH

Sequence of entity 2 (B, D, F, H), FASTA

>7VNR_2 Calmodulin-3 (chains B, D, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
7YV	(1S,2S,4R)-N-(2,4,6-trimethylphenyl)bicyclo[2.2.1]heptane-2-carboxamid	C17 H23 N O	4

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

Primary citation

Structural insights into the lipid and ligand regulation of a human neuronal KCNQ channel. Zheng, Y., Liu, H., Chen, Y. et al. Neuron (2022) 110:237. DOI 10.1016/j.neuron.2021.10.029 · PubMed

Other PDB entries of the same protein (UniProt P56696 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2OVC 2.07 Å, Crystal structure of a coiled-coil tetramerization domain from Kv7.4 channels
6N5W 2.15 Å, Crystal structure of the Ca2+/CaM complex with independent peptides of Kv7.4 (KCNQ4) A &…
6B8P 2.2 Å, Crystal Structure of the Mg2+/CaM:Kv7.4 (KCNQ4) AB domain complex
6B8N 2.2 Å, Crystal Structure of the Ca2+/CaM:Kv7.4 (KCNQ4) AB Domain Complex, 10 uM CaCl2 soak
6B8L 2.3 Å, Crystal Structure of the Apo/CaM:Kv7.4 (KCNQ4) AB Domain Complex
6B8M 2.3 Å, Crystal Structure of the Ca2+/CaM:Kv7.4 (KCNQ4) AB Domain Complex, 1 mM CaCl2 soak
7BYL 2.5 Å, Cryo-EM structure of human KCNQ4
4GOW 2.6 Å, Crystal Structure of Ca2+/CaM:Kv7.4 (KCNQ4) B helix complex
7VNP 2.79 Å, Structure of human KCNQ4-ML213 complex with PIP2
7VNQ 2.96 Å, Structure of human KCNQ4-ML213 complex in nanodisc
7BYM 3.1 Å, Cryo-EM structure of human KCNQ4 with retigabine
7BYN 3.3 Å, Cryo-EM structure of human KCNQ4 with linopirdine

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