Structure of human KCNQ4-ML213 complex with PIP2. Determined by electron microscopy at 2.79 Å resolution. Released 1 Dec 2021.
Explore 7VNP in 3D Show helices and sheets RCSB PDB PDBe
7VNP contains 100 α-helices and 0 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 | 75-92 | 18 | |
| α-helix | 96-98 | 3 | |
| α-helix | 99-120 | 22 | |
| α-helix | 126-152 | 27 | |
| α-helix | 162-171 | 10 | |
| α-helix | 173-190 | 18 | |
| α-helix | 201-215 | 15 | |
| α-helix | 223-233 | 11 | |
| α-helix | 235-260 | 26 | |
| α-helix | 270-281 | 12 | |
| α-helix | 294-311 | 18 | |
| α-helix | 313-355 | 43 | |
| α-helix | 529-536 | 8 | |
| α-helix | 537-541 | 5 | |
| α-helix | 542-551 | 10 | |
| α-helix | 557-561 | 5 | |
| α-helix | 562-583 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-19 | 13 | |
| α-helix | 30-40 | 11 | |
| α-helix | 46-55 | 10 | |
| α-helix | 68-72 | 5 | |
| α-helix | 80-93 | 14 | |
| α-helix | 103-112 | 10 | |
| α-helix | 119-128 | 10 | |
| α-helix | 139-147 | 9 |
| 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) |
>7VNP_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
>7VNP_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 |
| PT5 | [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4… | C47 H85 O19 P3 | 8 |
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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