9xb9

Human KCNQ2-CaM in complex with QO-58 and PIP2

Method: ELECTRON MICROSCOPY Dmax: 117.8 Å Quality: GOOD

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

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–872 Chain B; UniProt 1–872 Chain C; UniProt 1–872 Chain D; UniProt 1–872 Not recorded Calmodulin-1 × 4 (P0DP23) 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

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–872; UniProt 1–872 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

Calmodulin-1

Homo sapiens

UniProt P0DP23

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–149 Chain F; UniProt 1–149 Chain G; UniProt 1–149 Chain H; UniProt 1–149 Not recorded Potassium voltage-gated channel subfamily KQT member 2 × 4 (O43526) 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

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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–149; UniProt 1–149 Author chain F; PDBConstruct 1–149; UniProt 1–149 Author chain G; PDBConstruct 1–149; UniProt 1–149 Author chain H; PDBConstruct 1–149; UniProt 1–149

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 9xb9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xb9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9xb9
Deposition date deposition_date2025-10-23
Structure title titleHuman KCNQ2-CaM in complex with QO-58 and PIP2
Keywords keywordsvoltage-gated potassium channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.46
Radius of gyration Rg (electron density) rg_electron41.73
Forward intensity I(0) i0768582000.00
Molecular weight molecular_weight234650.0 kDa
Excluded volume excluded_volume295740 ų
Envelope volume envelope_volume400620 ų
Hydration-shell volume shell_volume76875 ų
Envelope diameter envelope_diameter126.5
Shell Rg shell_rg50.08
Envelope Rg envelope_rg40.61
Shape Rg shape_rg41.72
Total Rg total_rg42.18
Total atoms total_atoms32816
Residues n_residues2028
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 dmax117.8
Rg (real space) rg_real42.16
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real7.6860e+08
I(0) uncertainty (real space) i0_real_error1.2500e+07
Rg (reciprocal space) rg_reciprocal42.45
I(0) (reciprocal space) i0_reciprocal768800000.0000
Solution quality estimate total_estimate0.8556
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.1
Skewness Skewness skewness0.010
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45240000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.988; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.176

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)