7CR2: Human KCNQ2

human KCNQ2 in complex with retigabine. Determined by electron microscopy at 3.2 Å resolution. Released 16 Sept 2020.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,276
Mol. weight: 295.72 kDa
Ligands: FBX
Released: 16 Sept 2020

Explore 7CR2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CR2 contains 48 α-helices and 0 β-strands across 4 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, C and D: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	72-84	13
α-helix	92-112	21
α-helix	119-147	29
α-helix	148-150	3
α-helix	156-163	8
α-helix	167-182	16
α-helix	196-209	14
α-helix	216-227	12
α-helix	229-253	25
α-helix	264-275	12
α-helix	288-304	17
α-helix	307-329	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily KQT member 2	A, B, C, D	protein	656	Homo sapiens	O43526 (AlphaFold model)

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

>7CR2_1 Potassium voltage-gated channel subfamily KQT member 2 (chains A, B, C, D)
MAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSS
EGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAV
LAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLC
LILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGV
SFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQY
YERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCR
GPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPK
SWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRA
VCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDK
DRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAK
EPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSVEGGSSGGWSHPQFEK

Ligands and cofactors

ID	Name	Formula	Copies
FBX	ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate	C16 H18 F N3 O2	4

Primary citation

Molecular basis for ligand activation of the human KCNQ2 channel. Li, X., Zhang, Q., Guo, P. et al. Cell Res (2021) 31:52-61. DOI 10.1038/s41422-020-00410-8 · 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

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