6wth

Full-length human ENaC ECD

Method: ELECTRON MICROSCOPY Dmax: 145.5 Å Quality: GOOD

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

Amiloride-sensitive sodium channel subunit alpha

Homo sapiens

UniProt P37088

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–669 Not recorded Amiloride-sensitive sodium channel subunit beta × 1 (P51168) Amiloride-sensitive sodium channel subunit gamma × 1 (P51170) 7B1 Fab × 2 10D4 Fab × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 uL applied, manual blot, fresh 3.5 uL applied, vitrobot blot and freeze Resolution 3.06 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 SCNNA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–669; UniProt 1–669

Amiloride-sensitive sodium channel subunit beta

Homo sapiens

UniProt P51168

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–640 Not recorded Amiloride-sensitive sodium channel subunit alpha × 1 (P37088) Amiloride-sensitive sodium channel subunit gamma × 1 (P51170) 7B1 Fab × 2 10D4 Fab × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 uL applied, manual blot, fresh 3.5 uL applied, vitrobot blot and freeze Resolution 3.06 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCNNB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–640; UniProt 1–640

Amiloride-sensitive sodium channel subunit gamma

Homo sapiens

UniProt P51170

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–649 Not recorded Amiloride-sensitive sodium channel subunit alpha × 1 (P37088) Amiloride-sensitive sodium channel subunit beta × 1 (P51168) 7B1 Fab × 2 10D4 Fab × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 uL applied, manual blot, fresh 3.5 uL applied, vitrobot blot and freeze Resolution 3.06 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCNNG_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–649; UniProt 1–649

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 6wth

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wth
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wth
Deposition date deposition_date2020-05-02
Structure title titleFull-length human ENaC ECD
Keywords keywordssodium channel, blood pressure, epithelial, salt transport, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.06
Radius of gyration Rg (electron density) rg_electron37.79
Forward intensity I(0) i0459749000.00
Molecular weight molecular_weight166830.0 kDa
Excluded volume excluded_volume205230 ų
Envelope volume envelope_volume290820 ų
Hydration-shell volume shell_volume62740 ų
Envelope diameter envelope_diameter158.6
Shell Rg shell_rg43.99
Envelope Rg envelope_rg39.72
Shape Rg shape_rg37.91
Total Rg total_rg37.80
Total atoms total_atoms11740
Residues n_residues1594
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 dmax145.5
Rg (real space) rg_real39.25
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real4.5970e+08
I(0) uncertainty (real space) i0_real_error8.0980e+06
Rg (reciprocal space) rg_reciprocal39.13
I(0) (reciprocal space) i0_reciprocal459700000.0000
Solution quality estimate total_estimate0.8196
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.7
Skewness Skewness skewness0.584
Kurtosis Kurtosis kurtosis0.299
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119200000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.588; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)