8J02: PDB entry 8J02

Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state II. Determined by electron microscopy at 3.5 Å resolution. Released 13 Dec 2023.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 16,116
Mol. weight: 376.91 kDa
Ligands: PIO, P0T
Released: 13 Dec 2023

Explore 8J02 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8J02 contains 88 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	71-85	15
α-helix	92-114	23
α-helix	119-147	29
α-helix	156-164	9
α-helix	167-183	17
α-helix	196-210	15
α-helix	216-227	12
α-helix	229-253	25
α-helix	264-275	12
α-helix	288-348	61
α-helix	358-366	9
α-helix	536-558	23
α-helix	564-599	36

Chains C, E, F and H: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	27	1	1
α-helix	30-40	11
α-helix	46-56	11
β-strand	65	1	1
α-helix	66-74	9
α-helix	77-80	4
α-helix	84-93	10
β-strand	100-102	3	2
α-helix	103-110	8
α-helix	119-129	11
β-strand	136-138	3	2
α-helix	139-147	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily KQT member 2	A, B, D, G	protein	656	Homo sapiens	O43526 (AlphaFold model)
Calmodulin-1	C, E, F, H	protein	177	Homo sapiens	P0DP23 (AlphaFold model)

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

>8J02_1 Potassium voltage-gated channel subfamily KQT member 2 (chains A, B, D, G)
MAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVASCLVLSVFSTIKEYEKSS
EGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAV
LAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLC
LILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGV
SFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQY
YERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCR
GPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPK
SWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRA
VCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDK
DRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAK
EPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSVEGGSSGGWSHPQFEK

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

>8J02_2 Calmodulin-1 (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
P0T	cannabidiol	C21 H30 O2	4

Primary citation

Ligand activation mechanisms of human KCNQ2 channel. Ma, D., Zheng, Y., Li, X. et al. Nat Commun (2023) 14:6632-6632. DOI 10.1038/s41467-023-42416-x · PubMed

Other PDB entries of the same protein (UniProt O43526 (AlphaFold model), which also has an AlphaFold model), best resolution first:

22AY 2.3 Å, KCNQ2 homotetramer in apo state
22BJ 2.4 Å, KCNQ2/3 heterotetramer with 3:1 stoichiometry
22BF 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2
22BG 2.5 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
8IZY 2.5 Å, Human KCNQ2-CaM in complex with HN37
22BE 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
22BI 2.6 Å, XEN1101 bound KCNQ2/3 heteromer with 2:2 stoichiometry
22AZ 2.7 Å, ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1
22BK 2.7 Å, KCNQ2/3 heterotetramer with 2:2 stoichiometry
8J03 2.7 Å, Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state I
8J04 2.7 Å, Human KCNQ2-CaM-HN37 complex in the presence of PIP2
8J05 2.7 Å, Human KCNQ2-CaM complex in the presence of PIP2

Browse structure collections

About this viewer

MolViewer shows 8J02 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.