9czq

Ca2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in detergent.

Method: ELECTRON MICROSCOPY Dmax: 172.2 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 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 66–1121 Chain B; UniProt 66–1121 Chain C; UniProt 66–1121 Chain D; UniProt 66–1121 Not recorded Large-conductance Ca2+-activated K+ channel beta2 subunit,Calcium-activated potassium channel subunit beta-4 × 4 (B5BNX0,Q86W47) MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 20 CLR CHOLESTEROL × 11 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl pH 8.0, 450 mM KCl, 5 mM EDTA, 15 mM MgCl2, 0.02% GDN and 0.05 mg/ml POPE:POPC:POPA 5:5:1 (w:w:w). cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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 1–1056; UniProt 66–1121 Author chain B; PDBConstruct 1–1056; UniProt 66–1121 Author chain C; PDBConstruct 1–1056; UniProt 66–1121 Author chain D; PDBConstruct 1–1056; UniProt 66–1121

Large-conductance Ca2+-activated K+ channel beta2 subunit,Calcium-activated potassium channel subunit beta-4

Homo sapiens

UniProt B5BNX0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 2–44 Chain F; UniProt 2–44 Chain G; UniProt 2–44 Chain H; UniProt 2–44 Fragment:;N-terminal 45 residues of kcnmb2 ligated to kcnmb4 (devoid of N terminal first 15 residues),N-terminal 45 residues of kcnmb2 ligated to kcnmb4 (devoid of N terminal first 15 residues) ; Isoform 5 of Calcium-activated potassium channel subunit alpha-1 × 4 (Q12791) MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 20 CLR CHOLESTEROL × 11 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl pH 8.0, 450 mM KCl, 5 mM EDTA, 15 mM MgCl2, 0.02% GDN and 0.05 mg/ml POPE:POPC:POPA 5:5:1 (w:w:w). cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B5BNX0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–43; UniProt 2–44 Author chain F; PDBConstruct 1–43; UniProt 2–44 Author chain G; PDBConstruct 1–43; UniProt 2–44 Author chain H; PDBConstruct 1–43; UniProt 2–44

Large-conductance Ca2+-activated K+ channel beta2 subunit,Calcium-activated potassium channel subunit beta-4

Homo sapiens

UniProt Q86W47

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 15–210 Chain F; UniProt 15–210 Chain G; UniProt 15–210 Chain H; UniProt 15–210 Fragment:;N-terminal 45 residues of kcnmb2 ligated to kcnmb4 (devoid of N terminal first 15 residues),N-terminal 45 residues of kcnmb2 ligated to kcnmb4 (devoid of N terminal first 15 residues) ; Isoform 5 of Calcium-activated potassium channel subunit alpha-1 × 4 (Q12791) MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 20 CLR CHOLESTEROL × 11 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris-HCl pH 8.0, 450 mM KCl, 5 mM EDTA, 15 mM MgCl2, 0.02% GDN and 0.05 mg/ml POPE:POPC:POPA 5:5:1 (w:w:w). cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.88 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCMB4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 44–239; UniProt 15–210 Author chain F; PDBConstruct 44–239; UniProt 15–210 Author chain G; PDBConstruct 44–239; UniProt 15–210 Author chain H; PDBConstruct 44–239; UniProt 15–210

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 9czq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9czq
Deposition date deposition_date2024-08-05
Structure title titleCa2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in detergent.
Keywords keywords;Potassium ion channel, calcium and voltage gated ion channel, big potassium channel, human BK, hSlo1, open-inactivated hSlo1, ball and chain inactivation, hSlo1 inactivating subunit complex, detergent micelle, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.07
Radius of gyration Rg (electron density) rg_electron53.87
Forward intensity I(0) i03260700000.00
Molecular weight molecular_weight512410.0 kDa
Excluded volume excluded_volume653860 ų
Envelope volume envelope_volume942920 ų
Hydration-shell volume shell_volume139130 ų
Envelope diameter envelope_diameter168.9
Shell Rg shell_rg62.69
Envelope Rg envelope_rg52.28
Shape Rg shape_rg53.87
Total Rg total_rg54.11
Total atoms total_atoms36018
Residues n_residues4392
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 dmax172.2
Rg (real space) rg_real54.77
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real3.2610e+09
I(0) uncertainty (real space) i0_real_error6.9330e+07
Rg (reciprocal space) rg_reciprocal55.31
I(0) (reciprocal space) i0_reciprocal3263000000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.2
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha476900000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.783

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)