human KCNQ5-CaM in apo state. Determined by electron microscopy at 2.4 Å resolution. Released 16 Apr 2025.
Explore 9J38 in 3D Show helices and sheets RCSB PDB PDBe
9J38 contains 112 α-helices and 8 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 | 126-147 | 22 | |
| α-helix | 153-181 | 29 | |
| α-helix | 182-184 | 3 | |
| α-helix | 186-188 | 3 | |
| α-helix | 190-198 | 9 | |
| α-helix | 201-222 | 22 | |
| α-helix | 225-234 | 10 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-244 | 6 | |
| α-helix | 250-261 | 12 | |
| α-helix | 263-288 | 26 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-309 | 12 | |
| α-helix | 322-339 | 18 | |
| α-helix | 341-362 | 22 | |
| α-helix | 367-383 | 17 | |
| α-helix | 516-539 | 24 | |
| α-helix | 543-544 | 2 | |
| α-helix | 546-575 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| α-helix | 30-39 | 10 | |
| α-helix | 46-54 | 9 | |
| α-helix | 66-74 | 9 | |
| α-helix | 80-92 | 13 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-128 | 10 | |
| β-strand | 136-138 | 3 | 1 |
| α-helix | 140-147 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 5 | A, B, C, D | protein | 610 | Homo sapiens | Q9NR82 (AlphaFold model) |
| Calmodulin-1 | E, F, G, H | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
>9J38_1 Potassium voltage-gated channel subfamily KQT member 5 (chains A, B, C, D) MLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFST IPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTI VLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELIT AWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLS AGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSV SIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSP STDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCD VSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQ TRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQ QVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGL QFILTPNEFS
>9J38_2 Calmodulin-1 (chains E, F, G, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
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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