8vaz

Structure of human Slo1 and human LRRC26 in EDTA - LRRD masked

Method: ELECTRON MICROSCOPY Dmax: 157.0 Å Quality: GOOD

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

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 heterocomplex 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 Leucine-rich repeat-containing protein 26 × 4 (Q2I0M4) K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.82 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

Leucine-rich repeat-containing protein 26

Homo sapiens

UniProt Q2I0M4

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 1–334 Chain F; UniProt 1–334 Chain G; UniProt 1–334 Chain H; UniProt 1–334 Not recorded Calcium-activated potassium channel subunit alpha-1 × 4 (Q12791) K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.82 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRC26_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–334; UniProt 1–334 Author chain F; PDBConstruct 1–334; UniProt 1–334 Author chain G; PDBConstruct 1–334; UniProt 1–334 Author chain H; PDBConstruct 1–334; UniProt 1–334

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 8vaz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vaz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vaz
Deposition date deposition_date2023-12-11
Structure title titleStructure of human Slo1 and human LRRC26 in EDTA - LRRD masked
Keywords keywordsSlo1, BK, maxiK, potassium channel, voltage sensor, VSD, resting state, LRRC26, Gamma1, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.92
Radius of gyration Rg (electron density) rg_electron51.35
Forward intensity I(0) i02249020000.00
Molecular weight molecular_weight417660.0 kDa
Excluded volume excluded_volume530520 ų
Envelope volume envelope_volume778390 ų
Hydration-shell volume shell_volume120590 ų
Envelope diameter envelope_diameter156.9
Shell Rg shell_rg59.96
Envelope Rg envelope_rg49.67
Shape Rg shape_rg51.35
Total Rg total_rg51.61
Total atoms total_atoms29404
Residues n_residues3704
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 dmax157.0
Rg (real space) rg_real51.60
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real2.2490e+09
I(0) uncertainty (real space) i0_real_error4.2740e+07
Rg (reciprocal space) rg_reciprocal52.18
I(0) (reciprocal space) i0_reciprocal2251000000.0000
Solution quality estimate total_estimate0.8844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.3
Skewness Skewness skewness-0.028
Kurtosis Kurtosis kurtosis-0.566
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha287500000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.798

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)