8f75

LRRC8A(T48D):C conformation 2 LRR focus

Method: ELECTRON MICROSCOPY Dmax: 131.2 Å Quality: GOOD

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

Volume-regulated anion channel subunit LRRC8A

Mus musculus

UniProt Q80WG5

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 91–810 Chain B; UniProt 91–810 Not recorded Volume-regulated anion channel subunit LRRC8C × 1 (Q8R502) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRC8A_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–720; UniProt 91–810 Author chain B; PDBConstruct 1–720; UniProt 91–810

Volume-regulated anion channel subunit LRRC8C

Mus musculus

UniProt Q8R502

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–803 Not recorded Volume-regulated anion channel subunit LRRC8A × 2 (Q80WG5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRC8C_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–803; UniProt 1–803

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 8f75

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f75
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f75
Deposition date deposition_date2022-11-18
Structure title titleLRRC8A(T48D):C conformation 2 LRR focus
Keywords keywordsION CHANNEL, VOLUME-REGULATION, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.29
Radius of gyration Rg (electron density) rg_electron39.28
Forward intensity I(0) i0268607000.00
Molecular weight molecular_weight140550.0 kDa
Excluded volume excluded_volume179550 ų
Envelope volume envelope_volume240690 ų
Hydration-shell volume shell_volume52342 ų
Envelope diameter envelope_diameter131.1
Shell Rg shell_rg43.96
Envelope Rg envelope_rg38.21
Shape Rg shape_rg39.28
Total Rg total_rg39.61
Total atoms total_atoms9899
Residues n_residues1218
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 dmax131.2
Rg (real space) rg_real39.39
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real2.6860e+08
I(0) uncertainty (real space) i0_real_error4.4410e+06
Rg (reciprocal space) rg_reciprocal39.33
I(0) (reciprocal space) i0_reciprocal268600000.0000
Solution quality estimate total_estimate0.8754
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.9
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha31420000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)