← Back to search

Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：O43526 New Search
39PDB entries
39Biological assembly
129chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
22AY KCNQ2 homotetramer in apo state Deposited 2026-01-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.30 Å
22AZ ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.70 Å
22BA ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.90 Å
22BC ICA-1103811 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.80 Å
22BD ICA-1103811 bound KCNQ2/3 heteromer with 2:2 stoichiometry Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.00 Å
22BE XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 1 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.60 Å
22BF XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 2 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.50 Å
22BG XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.50 Å
22BH XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 4 Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.80 Å
22BI XEN1101 bound KCNQ2/3 heteromer with 2:2 stoichiometry Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.60 Å
22BJ KCNQ2/3 heterotetramer with 3:1 stoichiometry Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.40 Å
22BK KCNQ2/3 heterotetramer with 2:2 stoichiometry Deposited 2026-01-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain C 1–872（872 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 2.70 Å
5J03 Crystal Structure of a chimeric Kv7.2 - Kv7.3 proximal C-terminal Domain in Complex with Calmodulin Deposited 2016-03-26 Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 502–529（28 aa）
Not recorded CA CALCIUM ION × 5 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.7；292 K；18% PEG 4K and 100 mM calcium acetate
Resolution 2.00 Å R-free 0.228
6FEG Solution Structure of CaM/Kv7.2-hAB Complex Deposited 2018-01-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 326–372（47 aa）
Chain A 502–532（31 aa）
Mutation：Del. R374-K493,Del. R374-K493 Mutation：Del. R374-K493,Del. R374-K493 CA CALCIUM ION × 2 SOLUTION NMR
NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 120；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N; U-50% 2H] Kv7.2-hAB, 1 mM [U-100% 13C; U-100% 15N; U-50% 2H] Calmodulin, 120 mM potassium chloride, 20 mM MES, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 500 uM [U-100% 13C; U-100% 15N] Kv7.2-hAB, 500 uM Calmodulin, 120 mM potassium chloride, 20 mM MES, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 500 uM Kv7.2-hAB, 500 uM [U-100% 13C; U-100% 15N] Calmodulin, 120 mM potassium chloride, 20 mM MES, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 250 uM [U-100% 15N] Kv7.2-hAB, 250 uM [U-100% 15N] Calmodulin, 120 mM potassium chloride, 20 mM MES, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
6FEH Solution Structure of CaM/Kv7.2-hAB Complex Deposited 2018-01-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 326–372（47 aa）
Chain A 502–532（31 aa）
Mutation：Del. R374-K493,Del. R374-K493 Mutation：Del. R374-K493,Del. R374-K493 CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 120；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N; U-50% 2H] Kv7.2-hAB, 1 mM [U-100% 13C; U-100% 15N; U-50% 2H] Calmodulin, 120 mM potassium chloride, 20 mM MES, 5 mM CaCl2, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 500 uM [U-100% 13C; U-100% 15N] Kv7.2-hAB, 500 uM Calmodulin, 120 mM potassium chloride, 20 mM MES, 5 mM CaCl2, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 250 uM [U-100% 15N] Kv7.2-hAB, 250 uM [U-100% 15N] Calmodulin, 120 mM potassium chloride, 20 mM MES, 5 mM CaCl2, 2 uM sodium azide, 200 uM [U-2H] DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
7CR0 human KCNQ2 in apo state Deposited 2020-08-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
7CR1 human KCNQ2 in complex with ztz240 Deposited 2020-08-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded GB9 N-(6-chloranylpyridin-3-yl)-4-fluoranyl-benzamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7CR2 human KCNQ2 in complex with retigabine Deposited 2020-08-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded FBX ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7CR3 human KCNQ2-CaM in apo state Deposited 2020-08-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7CR4 human KCNQ2-CaM in complex with ztz240 Deposited 2020-08-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain F 64–702（639 aa）
Not recorded GB9 N-(6-chloranylpyridin-3-yl)-4-fluoranyl-benzamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
7CR7 human KCNQ2-CaM in complex with retigabine Deposited 2020-08-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded FBX ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
8IJK human KCNQ2-CaM-Ebio1 complex in the presence of PIP2 Deposited 2023-02-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded 7PN N-(1,2-dihydroacenaphthylen-5-yl)-4-fluoranyl-benzamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8IZY Human KCNQ2-CaM in complex with HN37 Deposited 2023-04-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded 9MF methyl N-[4-[(4-fluorophenyl)methyl-prop-2-ynyl-amino]-2,6-dimethyl-phenyl]carbamate × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8J00 Human KCNQ2-CaM in complex with CBD Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain C 64–702（639 aa）
Chain D 64–702（639 aa）
Not recorded P0T cannabidiol × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8J01 Human KCNQ2-CaM in complex with CBD and PIP2 Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded P0T cannabidiol × 8 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8J02 Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state II Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–703（640 aa）
Chain B 64–703（640 aa）
Chain D 64–703（640 aa）
Chain G 64–703（640 aa）
Not recorded P0T cannabidiol × 4 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8J03 Human KCNQ2(F104A)-CaM-PIP2-CBD complex in state I Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–703（640 aa）
Chain D 64–703（640 aa）
Chain G 64–703（640 aa）
Chain I 64–703（640 aa）
Not recorded P0T cannabidiol × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
8J04 Human KCNQ2-CaM-HN37 complex in the presence of PIP2 Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded 9MF methyl N-[4-[(4-fluorophenyl)methyl-prop-2-ynyl-amino]-2,6-dimethyl-phenyl]carbamate × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
8J05 Human KCNQ2-CaM complex in the presence of PIP2 Deposited 2023-04-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
8W4U human KCNQ2-CaM in complex with PIP2 and HN37 Deposited 2023-08-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain B 64–702（639 aa）
Chain D 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded 9MF methyl N-[4-[(4-fluorophenyl)methyl-prop-2-ynyl-amino]-2,6-dimethyl-phenyl]carbamate × 4 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8X43 human KCNQ2-CaM-Ebio1-S1 complex in the presence of PIP2 Deposited 2023-11-15 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–702（639 aa）
Chain C 64–702（639 aa）
Chain E 64–702（639 aa）
Chain G 64–702（639 aa）
Not recorded 7Q0 N-(4-azanyl-1,2-dihydroacenaphthylen-5-yl)-4-fluoranyl-benzamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8XO1 Human KCNQ2-CaM in complex with QO-83 Deposited 2023-12-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded A1LWZ ~{N}-[2-azanyl-3-fluoranyl-4-[[4-(trifluoromethyl)phenyl]methylamino]phenyl]-3-cyclopentyl-propanamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9IXY Human KCNQ2-CaM-Ebio2 Complex in the Presence of PIP2 Deposited 2024-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–674（611 aa）
Chain B 64–674（611 aa）
Chain C 64–674（611 aa）
Chain D 64–674（611 aa）
Not recorded A1L3C ~{N}-[7-[bis(fluoranyl)methoxy]-1-prop-2-ynyl-indazol-3-yl]-3,3-dimethyl-butanamide × 4 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9IXZ human KCNQ2-CaM-Ebio3 Complex in the Presence of PIP2 Deposited 2024-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 64–674（611 aa）
Chain B 64–674（611 aa）
Chain C 64–674（611 aa）
Chain D 64–674（611 aa）
Not recorded A1L3D ~{N}-[7-[bis(fluoranyl)methoxy]-1-prop-2-ynyl-indazol-3-yl]-2-propyl-pentanamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9L8W Human KCNQ2-CaM in complex with QO-58 Deposited 2024-12-28 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded A1LVR QO-58 × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9X5J Cryo-EM structure of the human KCNQ2/3 heteromer channel Deposited 2025-10-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain D 70–594（525 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions Resolution 3.05 Å
9X65 Cryo-EM structure of the human KCNQ2/3 heteromer channel in the XEN1101-bound open state Deposited 2025-10-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain D 1–872（872 aa）
Not recorded A1EY8 Azetukalner × 4 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 K POTASSIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.19 Å
9XB9 Human KCNQ2-CaM in complex with QO-58 and PIP2 Deposited 2025-10-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 A1LVR QO-58 × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9XED Human KCNQ2-CaM in complex with QO-83 and PIP2 Deposited 2025-10-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 1–872（872 aa）
Chain B 1–872（872 aa）
Chain C 1–872（872 aa）
Chain D 1–872（872 aa）
Not recorded PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 A1LWZ ~{N}-[2-azanyl-3-fluoranyl-4-[[4-(trifluoromethyl)phenyl]methylamino]phenyl]-3-cyclopentyl-propanamide × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.