8f0s

Structure of VSD4-NaV1.7-NaVPas channel chimera bound to the hybrid inhibitor GNE-9296

Method: ELECTRON MICROSCOPY Dmax: 114.1 Å Quality: GOOD

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

Sodium channel protein PaFPC1,Sodium channel protein type 9 subunit alpha chimera

Homo sapiens

UniProt D0E0C2

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 × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1155 Chain A; UniProt 1286–1553 Fragment:Chimeric construct of human Nav1.7 VSD4 and the NavPaS channel from American cockroach Periplaneta americana Beta-diguetoxin-Dc1a × 1 (P49126) ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X80 5-chloro-4-(cyclopentylmethoxy)-N-(4-{[(1S,2S)-2-(dimethylamino)cyclohexyl]amino}-2-fluorobenzene-1-sulfonyl)-2-fluorobenzamide × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCNA1_PERAM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 56–1210; UniProt 1–1155 Author chain A; PDBConstruct 1341–1608; UniProt 1286–1553

Sodium channel protein PaFPC1,Sodium channel protein type 9 subunit alpha chimera

Homo sapiens

UniProt Q15858

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 × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1501–1630 Fragment:Chimeric construct of human Nav1.7 VSD4 and the NavPaS channel from American cockroach Periplaneta americana Beta-diguetoxin-Dc1a × 1 (P49126) ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X80 5-chloro-4-(cyclopentylmethoxy)-N-(4-{[(1S,2S)-2-(dimethylamino)cyclohexyl]amino}-2-fluorobenzene-1-sulfonyl)-2-fluorobenzamide × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

42 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCN9A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1211–1340; UniProt 1501–1630

Beta-diguetoxin-Dc1a

Diguetia canities

UniProt P49126

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 × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 39–94 Not recorded Sodium channel protein PaFPC1,Sodium channel protein type 9 subunit alpha chimera × 1 (D0E0C2,Q15858) ;beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X80 5-chloro-4-(cyclopentylmethoxy)-N-(4-{[(1S,2S)-2-(dimethylamino)cyclohexyl]amino}-2-fluorobenzene-1-sulfonyl)-2-fluorobenzamide × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TXI92_DIGCA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 16–71; UniProt 39–94

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 8f0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f0s
Deposition date deposition_date2022-11-03
最后修订 last_revision2023-04-12
Structure title titleStructure of VSD4-NaV1.7-NaVPas channel chimera bound to the hybrid inhibitor GNE-9296
Keywords keywordsIon channel, small molecule, inhibitor, MEMBRANE PROTEIN-INHIBITOR complex; MEMBRANE PROTEIN/INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.89
Radius of gyration Rg (electron density) rg_electron35.02
Forward intensity I(0) i0236055000.00
Molecular weight molecular_weight137950.0 kDa
Excluded volume excluded_volume178230 ų
Envelope volume envelope_volume232900 ų
Hydration-shell volume shell_volume54473 ų
Envelope diameter envelope_diameter123.3
Shell Rg shell_rg42.26
Envelope Rg envelope_rg35.15
Shape Rg shape_rg34.99
Total Rg total_rg35.67
Total atoms total_atoms9734
Residues n_residues1158
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 dmax114.1
Rg (real space) rg_real35.69
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real2.3610e+08
I(0) uncertainty (real space) i0_real_error3.8200e+06
Rg (reciprocal space) rg_reciprocal35.81
I(0) (reciprocal space) i0_reciprocal236100000.0000
Solution quality estimate total_estimate0.8842
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.3
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23960000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)