9wd8

structure of human KCNQ1-KCNE3-CaM complex with two PIP2

Method: ELECTRON MICROSCOPY Dmax: 127.7 Å Quality: GOOD

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

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–149 Chain E; UniProt 1–149 Chain H; UniProt 1–149 Chain K; UniProt 1–149 Not recorded Potassium voltage-gated channel subfamily E member 3 × 4 (Q9Y6H6) Potassium voltage-gated channel subfamily KQT member 1 × 4 (P51787) CA CALCIUM ION × 8 A1BBG (2R)-3-{[(S)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl di[(9Z)-octadec-9-enoate] × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1
Chains and sequence ranges Author chain B; PDBConstruct 1–149; UniProt 1–149 Author chain E; PDBConstruct 1–149; UniProt 1–149 Author chain H; PDBConstruct 1–149; UniProt 1–149 Author chain K; PDBConstruct 1–149; UniProt 1–149

Potassium voltage-gated channel subfamily E member 3

Homo sapiens

UniProt Q9Y6H6

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–103 Chain F; UniProt 1–103 Chain I; UniProt 1–103 Chain L; UniProt 1–103 Not recorded Calmodulin-1 × 4 (P0DP23) Potassium voltage-gated channel subfamily KQT member 1 × 4 (P51787) CA CALCIUM ION × 8 A1BBG (2R)-3-{[(S)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl di[(9Z)-octadec-9-enoate] × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNE3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103 Author chain I; PDBConstruct 1–103; UniProt 1–103 Author chain L; PDBConstruct 1–103; UniProt 1–103

Potassium voltage-gated channel subfamily KQT member 1

Homo sapiens

UniProt P51787

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 76–620 Chain D; UniProt 76–620 Chain G; UniProt 76–620 Chain J; UniProt 76–620 Not recorded Calmodulin-1 × 4 (P0DP23) Potassium voltage-gated channel subfamily E member 3 × 4 (Q9Y6H6) CA CALCIUM ION × 8 A1BBG (2R)-3-{[(S)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl di[(9Z)-octadec-9-enoate] × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

26 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNQ1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 2–546; UniProt 76–620 Author chain D; PDBConstruct 2–546; UniProt 76–620 Author chain G; PDBConstruct 2–546; UniProt 76–620 Author chain J; PDBConstruct 2–546; UniProt 76–620

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 9wd8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wd8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9wd8
Deposition date deposition_date2025-08-18
Structure title titlestructure of human KCNQ1-KCNE3-CaM complex with two PIP2
Keywords keywordspotassium channel complex, membrane protein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.58
Radius of gyration Rg (electron density) rg_electron40.89
Forward intensity I(0) i01378340000.00
Molecular weight molecular_weight206250.0 kDa
Excluded volume excluded_volume201110 ų
Envelope volume envelope_volume404390 ų
Hydration-shell volume shell_volume78714 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg49.09
Envelope Rg envelope_rg40.61
Shape Rg shape_rg40.86
Total Rg total_rg41.25
Total atoms total_atoms15660
Residues n_residues2060
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 dmax127.7
Rg (real space) rg_real41.34
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.3780e+09
I(0) uncertainty (real space) i0_real_error2.2180e+07
Rg (reciprocal space) rg_reciprocal41.58
I(0) (reciprocal space) i0_reciprocal1379000000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.8
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71720000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)