10ad

Cryo-EM structure of the human BK channel bound to the agonist NS1619

Method: ELECTRON MICROSCOPY Dmax: 151.1 Å Quality: GOOD

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

Isoform 5 of Calcium-activated potassium channel subunit alpha-1

Homo sapiens

UniProt Q12791

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 66–1178 Chain C; UniProt 66–1178 Chain D; UniProt 66–1178 Chain E; UniProt 66–1178 Not recorded MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 A1E02 3-[2-oxidanyl-5-(trifluoromethyl)phenyl]-6-(trifluoromethyl)-1~{H}-benzimidazol-2-one × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

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

View Construct and Data Evidence
UniProt name KCMA1_HUMAN
Isoform Q12791-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1113; UniProt 66–1178 Author chain C; PDBConstruct 1–1113; UniProt 66–1178 Author chain D; PDBConstruct 1–1113; UniProt 66–1178 Author chain E; PDBConstruct 1–1113; UniProt 66–1178

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 10ad

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ad
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ad
Deposition date deposition_date2026-01-08
Structure title titleCryo-EM structure of the human BK channel bound to the agonist NS1619
Keywords keywordsBK, Slo1, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.97
Radius of gyration Rg (electron density) rg_electron49.41
Forward intensity I(0) i02015090000.00
Molecular weight molecular_weight398070.0 kDa
Excluded volume excluded_volume506500 ų
Envelope volume envelope_volume713620 ų
Hydration-shell volume shell_volume114590 ų
Envelope diameter envelope_diameter158.3
Shell Rg shell_rg58.80
Envelope Rg envelope_rg47.57
Shape Rg shape_rg49.34
Total Rg total_rg49.96
Total atoms total_atoms55972
Residues n_residues3496
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 dmax151.1
Rg (real space) rg_real49.66
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real2.0150e+09
I(0) uncertainty (real space) i0_real_error3.3750e+07
Rg (reciprocal space) rg_reciprocal50.22
I(0) (reciprocal space) i0_reciprocal2017000000.0000
Solution quality estimate total_estimate0.8850
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.8
Skewness Skewness skewness-0.062
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha256100000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)