22bg

XEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium voltage-gated channel subfamily KQT member 3

Homo sapiens

UniProt O43525

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–872 Not recorded Potassium voltage-gated channel subfamily KQT member 2 × 3 (O43526) POTASSIUM ION × 3 Azetukalner × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNQ3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–872; UniProt 1–872

Potassium voltage-gated channel subfamily KQT member 2

Homo sapiens

UniProt O43526

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–872 Chain C; UniProt 1–872 Chain D; UniProt 1–872 Not recorded Potassium voltage-gated channel subfamily KQT member 3 × 1 (O43525) POTASSIUM ION × 3 Azetukalner × 4 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

38 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNQ2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–872; UniProt 1–872 Author chain C; PDBConstruct 1–872; UniProt 1–872 Author chain D; PDBConstruct 1–872; UniProt 1–872

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 22bg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 22bg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id22bg
Deposition date deposition_date2026-01-05
Structure title titleXEN1101 bound KCNQ2/3 heteromer with 3:1 stoichiometry, state 3
Keywords keywordsM-channel, KCNQ2/3, heteromeric channel, cryoEM, XEN1101, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.03
Radius of gyration Rg (electron density) rg_electron33.22
Forward intensity I(0) i0353496000.00
Molecular weight molecular_weight106560.0 kDa
Excluded volume excluded_volume106130 ų
Envelope volume envelope_volume193270 ų
Hydration-shell volume shell_volume48175 ų
Envelope diameter envelope_diameter116.0
Shell Rg shell_rg40.26
Envelope Rg envelope_rg33.46
Shape Rg shape_rg33.20
Total Rg total_rg33.67
Total atoms total_atoms8139
Residues n_residues989
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax108.8
Rg (real space) rg_real33.91
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real3.5350e+08
I(0) uncertainty (real space) i0_real_error5.7710e+06
Rg (reciprocal space) rg_reciprocal33.98
I(0) (reciprocal space) i0_reciprocal353500000.0000
Solution quality estimate total_estimate0.8824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.3
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27490000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)