9dx7

LRRC8A:D Conformation 1

Method: ELECTRON MICROSCOPY Dmax: 123.1 Å Quality: GOOD

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

Volume-regulated anion channel subunit LRRC8A,Soluble cytochrome b562

Mus musculus

UniProt P0ABE8

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 23–127 Chain B; UniProt 23–127 Chain C; UniProt 23–127 Chain D; UniProt 23–127 Not recorded Volume-regulated anion channel subunit LRRC8D × 2 (Q8BGR2) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C562_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 77–181; UniProt 23–127 Author chain B; PDBConstruct 77–181; UniProt 23–127 Author chain C; PDBConstruct 77–181; UniProt 23–127 Author chain D; PDBConstruct 77–181; UniProt 23–127

Volume-regulated anion channel subunit LRRC8A,Soluble cytochrome b562

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 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–76 Chain A; UniProt 91–810 Chain B; UniProt 1–76 Chain B; UniProt 91–810 Chain C; UniProt 1–76 Chain C; UniProt 91–810 Chain D; UniProt 1–76 Chain D; UniProt 91–810 Not recorded Volume-regulated anion channel subunit LRRC8D × 2 (Q8BGR2) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 1–76; UniProt 1–76 Author chain A; PDBConstruct 183–902; UniProt 91–810 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 183–902; UniProt 91–810 Author chain C; PDBConstruct 1–76; UniProt 1–76 Author chain C; PDBConstruct 183–902; UniProt 91–810 Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 183–902; UniProt 91–810

Volume-regulated anion channel subunit LRRC8D

Mus musculus

UniProt Q8BGR2

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–859 Chain F; UniProt 1–859 Not recorded Volume-regulated anion channel subunit LRRC8A,Soluble cytochrome b562 × 4 (Q80WG5,P0ABE8) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRC8D_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–859; UniProt 1–859 Author chain F; PDBConstruct 1–859; UniProt 1–859

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 9dx7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dx7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dx7
Deposition date deposition_date2024-10-10
Structure title titleLRRC8A:D Conformation 1
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_guinier42.04
Radius of gyration Rg (electron density) rg_electron40.26
Forward intensity I(0) i0643618000.00
Molecular weight molecular_weight230030.0 kDa
Excluded volume excluded_volume296680 ų
Envelope volume envelope_volume400410 ų
Hydration-shell volume shell_volume80271 ų
Envelope diameter envelope_diameter130.0
Shell Rg shell_rg48.29
Envelope Rg envelope_rg38.82
Shape Rg shape_rg40.27
Total Rg total_rg40.69
Total atoms total_atoms16238
Residues n_residues1873
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 dmax123.1
Rg (real space) rg_real41.79
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real6.4360e+08
I(0) uncertainty (real space) i0_real_error1.1290e+07
Rg (reciprocal space) rg_reciprocal42.04
I(0) (reciprocal space) i0_reciprocal643800000.0000
Solution quality estimate total_estimate0.8759
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.3
Skewness Skewness skewness0.050
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71420000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.502

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)