Human KCNQ5-CaM in complex with PIP2. Determined by electron microscopy at 3.1 Å resolution. Released 16 Apr 2025.
Explore 9LIZ in 3D Show helices and sheets RCSB PDB PDBe
9LIZ 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 | 104-120 | 17 | |
| α-helix | 125-148 | 24 | |
| α-helix | 153-180 | 28 | |
| α-helix | 190-198 | 9 | |
| α-helix | 201-222 | 22 | |
| α-helix | 225-234 | 10 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-245 | 7 | |
| α-helix | 250-261 | 12 | |
| α-helix | 263-288 | 26 | |
| α-helix | 298-309 | 12 | |
| α-helix | 322-362 | 41 | |
| α-helix | 367-383 | 17 | |
| α-helix | 516-540 | 25 | |
| α-helix | 543-544 | 2 | |
| α-helix | 546-575 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| β-strand | 27-28 | 2 | 3 |
| α-helix | 30-38 | 9 | |
| α-helix | 46-54 | 9 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 66-74 | 9 | |
| α-helix | 80-91 | 12 | |
| β-strand | 101-102 | 2 | 4 |
| α-helix | 103-112 | 10 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-127 | 9 | |
| β-strand | 136-137 | 2 | 4 |
| α-helix | 139-146 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 5 | A, B, D, G | protein | 626 | Homo sapiens | Q9NR82 (AlphaFold model) |
| Calmodulin-3 | C, E, F, H | protein | 177 | Homo sapiens | P0DP25 (AlphaFold model) |
>9LIZ_1 Potassium voltage-gated channel subfamily KQT member 5 (chains A, B, D, G) MLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFST IPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTI VLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELIT AWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLS AGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSV SIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSP STDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCD VSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQ TRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQ QVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGL QFILTPNEFSLEGGSSGGWSHPQFEK
>9LIZ_2 Calmodulin-3 (chains C, E, F, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| PIO | [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d… | C25 H49 O19 P3 | 4 |
Phosphatidylinositol 4,5-bisphosphate activation mechanism of human KCNQ5. Yang, Z., Zheng, Y., Ma, D. et al. Proc Natl Acad Sci U S A (2025) 122:e2416738122-e2416738122. DOI 10.1073/pnas.2416738122 · PubMed
Other PDB entries of the same protein (UniProt Q9NR82 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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