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7yo1

Cryo-EM structure of RCK1 mutated human Slo1-LRRC26 complex

Method: ELECTRON MICROSCOPY Dmax: 180.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Calcium-activated potassium channel subunit alpha-1

Homo sapiens

UniProt A0A1W2PRB0

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 66–1125 Chain C； UniProt 66–1125 Chain E； UniProt 66–1125 Chain G； UniProt 66–1125 Mutation：D372A, D367A, K577S Leucine-rich repeat-containing protein 26 × 4 （Q2I0M4） MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.60 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.

Other PDB Difference from Current Entry 7YO1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7YNZ Cryo-EM structure of human Slo1-LRRC26 complex with C1 symmetry Deposited 2022-08-01 Different mutation/modification Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 66–1125（1060 aa）
Chain C 66–1125（1060 aa）
Chain E 66–1125（1060 aa）
Chain G 66–1125（1060 aa）
Mutation：K577S Mutation：K577S Mutation：K577S Mutation：K577S MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
7YO0 Cryo-EM structure of human Slo1-LRRC26 complex with Symmetry Expansion Deposited 2022-08-01 Different mutation/modification Different ligand/ion Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 66–1125（1060 aa）
Chain C 66–1125（1060 aa）
Chain E 66–1125（1060 aa）
Chain G 66–1125（1060 aa）
Mutation：K577S Mutation：K577S Mutation：K577S Mutation：K577S PGW (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7YO2 Cryo-EM structure of RCK1-RCK2 mutated human Slo1 apo Deposited 2022-08-01 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 66–1125（1060 aa）
Chain B 66–1125（1060 aa）
Chain C 66–1125（1060 aa）
Chain D 66–1125（1060 aa）
Mutation：D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation：D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation：D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation：D362A, D367A, D894N, D895N, D896N, D897N, D898N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7YO3 Cryo-EM structure of human Slo1-LRRC26 complex with C4 symmetry Deposited 2022-08-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 66–1125（1060 aa）
Mutation：K577S MG MAGNESIUM ION × 1 CA CALCIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
7YO4 Cryo-EM structure of RCK1-RCK2 mutated human Slo1-LRRC26 complex Deposited 2022-08-01 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 66–1125（1060 aa）
Chain C 66–1125（1060 aa）
Chain E 66–1125（1060 aa）
Chain G 66–1125（1060 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
7YO5 Cryo-EM structure of RCK1 mutated human Slo1 apo Deposited 2022-08-01 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 66–1125（1060 aa）
Chain B 66–1125（1060 aa）
Chain C 66–1125（1060 aa）
Chain D 66–1125（1060 aa）
Mutation：D362A, D367A, K577S Mutation：D362A, D367A, K577S Mutation：D362A, D367A, K577S Mutation：D362A, D367A, K577S CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å

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

View Construct and Data Evidence
UniProt name A0A1W2PRB0_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–1060； UniProt 66–1125 Author chain C； PDBConstruct 1–1060； UniProt 66–1125 Author chain E； PDBConstruct 1–1060； UniProt 66–1125 Author chain G； PDBConstruct 1–1060； UniProt 66–1125

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 B； UniProt 1–334 Chain D； UniProt 1–334 Chain F； UniProt 1–334 Chain H； UniProt 1–334 Not recorded Calcium-activated potassium channel subunit alpha-1 × 4 （A0A1W2PRB0） MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.60 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.

Other PDB Difference from Current Entry 7YO1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7YNZ Cryo-EM structure of human Slo1-LRRC26 complex with C1 symmetry Deposited 2022-08-01 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–334（334 aa）
Chain D 1–334（334 aa）
Chain F 1–334（334 aa）
Chain H 1–334（334 aa）
Not recorded MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
7YO0 Cryo-EM structure of human Slo1-LRRC26 complex with Symmetry Expansion Deposited 2022-08-01 Different ligand/ion Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–334（334 aa）
Chain D 1–334（334 aa）
Chain F 1–334（334 aa）
Chain H 1–334（334 aa）
Not recorded PGW (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7YO3 Cryo-EM structure of human Slo1-LRRC26 complex with C4 symmetry Deposited 2022-08-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–334（334 aa）
Not recorded MG MAGNESIUM ION × 1 CA CALCIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
7YO4 Cryo-EM structure of RCK1-RCK2 mutated human Slo1-LRRC26 complex Deposited 2022-08-01 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–334（334 aa）
Chain D 1–334（334 aa）
Chain F 1–334（334 aa）
Chain H 1–334（334 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
8VAV Human Slo1 - human LRRC26 in presence of EDTA - GR masked Deposited 2023-12-11 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 1–334（334 aa）
Chain F 1–334（334 aa）
Chain G 1–334（334 aa）
Chain H 1–334（334 aa）
Not recorded POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 20 K POTASSIUM ION × 4 AJP Digitonin × 32 CLR CHOLESTEROL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.13 Å
8VAZ Structure of human Slo1 and human LRRC26 in EDTA - LRRD masked Deposited 2023-12-11 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 1–334（334 aa）
Chain F 1–334（334 aa）
Chain G 1–334（334 aa）
Chain H 1–334（334 aa）
Not recorded K POTASSIUM ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.82 Å

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 B； PDBConstruct 1–334； UniProt 1–334 Author chain D； PDBConstruct 1–334； UniProt 1–334 Author chain F； 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 7yo1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yo1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7yo1
Deposition date deposition_date2022-08-01
Structure title titleCryo-EM structure of RCK1 mutated human Slo1-LRRC26 complex
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier58.55 Å
Radius of gyration Rg (electron density) rg_electron57.69 Å
Forward intensity I(0) i03342730000.00
Molecular weight molecular_weight508740.0 kDa
Excluded volume excluded_volume645540 ų
Envelope volume envelope_volume976130 ų
Hydration-shell volume shell_volume137440 ų
Envelope diameter envelope_diameter178.4 Å
Shell Rg shell_rg64.00 Å
Envelope Rg envelope_rg55.55 Å
Shape Rg shape_rg57.64 Å
Total Rg total_rg58.01 Å
Total atoms total_atoms35800
Residues n_residues4568
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax180.8 Å
Rg (real space) rg_real58.28 Å
Rg uncertainty (real space) rg_real_error1.56 Å
I(0) (real space) i0_real3.3430e+09
I(0) uncertainty (real space) i0_real_error6.3590e+07
Rg (reciprocal space) rg_reciprocal58.75 Å
I(0) (reciprocal space) i0_reciprocal3345000000.0000
Solution quality estimate total_estimate0.8310
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.7 Å
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.1350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha223300000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)