9LJ1: PDB entry 9LJ1

Human KCNQ5-CaM-PIP2-HN37 complex in a closed conformation. Determined by electron microscopy at 3.2 Å resolution. Released 16 Apr 2025.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 8
Atoms: 15,884
Mol. weight: 364.66 kDa
Ligands: PIO, 9MF
Released: 16 Apr 2025

Explore 9LJ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LJ1 contains 96 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.

Chains A, B, D and G: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	104-120	17
α-helix	125-148	24
α-helix	153-184	32
α-helix	190-198	9
α-helix	201-222	22
α-helix	225-236	12
α-helix	237-239	3
α-helix	240-245	6
α-helix	247-249	3
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	516-541	26
α-helix	546-575	30

Chains C, E, F and H: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-21	15
β-strand	27-28	2	3
α-helix	30-38	9
α-helix	46-56	11
β-strand	64-65	2	3
α-helix	66-74	9
α-helix	80-92	13
β-strand	100-102	3	4
α-helix	103-112	10
α-helix	119-128	10
β-strand	136-138	3	4
α-helix	139-146	8

Molecules and chains

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)

Sequence of entity 1 (A, B, D, G), FASTA

>9LJ1_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

Sequence of entity 2 (C, E, F, H), FASTA

>9LJ1_2 Calmodulin-3 (chains C, E, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAKLEGGSSGGLVPRGSGGSSGGHHHHHHHH

Ligands and cofactors

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
9MF	methyl N-[4-[(4-fluorophenyl)methyl-prop-2-ynyl-amino]-2,6-dimethyl-phenyl]carb…	C20 H21 F N2 O2	4

Primary citation

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:

9J38 2.4 Å, human KCNQ5-CaM in apo state
6B8Q 2.6 Å, Crystal Structure of the Mg2+/CaM:Kv7.5 (KCNQ5) AB domain complex
9LJ5 2.9 Å, Human KCNQ5-CaM-PIP2-HN37 complex in an open conformation.
9LIZ 3.1 Å, Human KCNQ5-CaM in complex with PIP2

Browse structure collections

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