9czm

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

Method: ELECTRON MICROSCOPY Dmax: 168.7 Å Quality: REASONABLE

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

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 Not recorded Isoform 5 of Calcium-activated potassium channel subunit alpha-1 × 4 (Q12791) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 32 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 CLR CHOLESTEROL × 8 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 2.57 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 1
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 Not recorded Isoform 5 of Calcium-activated potassium channel subunit alpha-1 × 4 (Q12791) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 32 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 CLR CHOLESTEROL × 8 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 2.57 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 1
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

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) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 32 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 CLR CHOLESTEROL × 8 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 2.57 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 2
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

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 9czm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9czm
Deposition date deposition_date2024-08-05
Structure title titleCa2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in nanodisc.
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, beta2 beta4, nanodisc, membrane protein ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.92
Radius of gyration Rg (electron density) rg_electron53.69
Forward intensity I(0) i03258270000.00
Molecular weight molecular_weight513060.0 kDa
Excluded volume excluded_volume654980 ų
Envelope volume envelope_volume933770 ų
Hydration-shell volume shell_volume137860 ų
Envelope diameter envelope_diameter167.9
Shell Rg shell_rg62.72
Envelope Rg envelope_rg52.16
Shape Rg shape_rg53.70
Total Rg total_rg53.90
Total atoms total_atoms36052
Residues n_residues4367
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 dmax168.7
Rg (real space) rg_real54.62
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real3.2580e+09
I(0) uncertainty (real space) i0_real_error5.7990e+07
Rg (reciprocal space) rg_reciprocal55.16
I(0) (reciprocal space) i0_reciprocal3261000000.0000
Solution quality estimate total_estimate0.6436
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.8
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha483500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 0.001; Positv: 1.000; Valcen: 0.954; Smooth: 0.613

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)