Structure of human KCNQ4-ML213 complex in nanodisc. Determined by electron microscopy at 2.96 Å resolution. Released 1 Dec 2021.
Explore 7VNQ in 3D Show helices and sheets RCSB PDB PDBe
7VNQ contains 100 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 75-95 | 21 | |
| α-helix | 98-120 | 23 | |
| α-helix | 126-153 | 28 | |
| α-helix | 163-168 | 6 | |
| α-helix | 174-187 | 14 | |
| α-helix | 188-192 | 5 | |
| α-helix | 200-215 | 16 | |
| α-helix | 223-233 | 11 | |
| α-helix | 235-260 | 26 | |
| α-helix | 270-281 | 12 | |
| α-helix | 294-307 | 14 | |
| α-helix | 310-312 | 3 | |
| α-helix | 313-334 | 22 | |
| α-helix | 339-354 | 16 | |
| α-helix | 533-550 | 18 | |
| α-helix | 560-586 | 27 |
| 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 |
| 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) |
>7VNQ_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
>7VNQ_2 Calmodulin-3 (chains B, D, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
| 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.
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:
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