25ij

Cryo-EM structure of human Nav1.6 in complex with delta-paraponeritoxin-Pc1a

Method: ELECTRON MICROSCOPY Dmax: 136.5 Å Quality: GOOD

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

Sodium channel protein type 8 subunit alpha

Homo sapiens

UniProt Q9UQD0

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1980 Not recorded Delta-paraponeritoxin-Pc1a × 1 (P41736) Sodium channel regulatory subunit beta-1 × 1 (Q07699) ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-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 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 Y01 CHOLESTEROL HEMISUCCINATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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

View Construct and Data Evidence
UniProt name SCN8A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1980; UniProt 1–1980

Delta-paraponeritoxin-Pc1a

Paraponera clavata

UniProt P41736

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–25 Non-standard monomer:Yes (specific site not provided by mmCIF) Sodium channel protein type 8 subunit alpha × 1 (Q9UQD0) Sodium channel regulatory subunit beta-1 × 1 (Q07699) ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-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 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 Y01 CHOLESTEROL HEMISUCCINATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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

View Construct and Data Evidence
UniProt name TX1A_PARCV
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 1–25

Sodium channel regulatory subunit beta-1

Homo sapiens

UniProt Q07699

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 × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 20–192 Not recorded Sodium channel protein type 8 subunit alpha × 1 (Q9UQD0) Delta-paraponeritoxin-Pc1a × 1 (P41736) ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-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 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 Y01 CHOLESTEROL HEMISUCCINATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

38 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCN1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–173; UniProt 20–192

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 25ij

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 25ij
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2. Structure Basics 2. Structure Basics

Entry ID entry_id25ij
Deposition date deposition_date2026-04-06
Structure title titleCryo-EM structure of human Nav1.6 in complex with delta-paraponeritoxin-Pc1a
Keywords keywordsNav1.6, voltage gated sodium channel, toxin, Pc1a, delta-paraponeritoxin-Pc1a, TRANSPORT PROTEIN, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.73
Radius of gyration Rg (electron density) rg_electron40.04
Forward intensity I(0) i0371479000.00
Molecular weight molecular_weight173750.0 kDa
Excluded volume excluded_volume224240 ų
Envelope volume envelope_volume308170 ų
Hydration-shell volume shell_volume64062 ų
Envelope diameter envelope_diameter145.1
Shell Rg shell_rg45.35
Envelope Rg envelope_rg40.35
Shape Rg shape_rg40.07
Total Rg total_rg40.28
Total atoms total_atoms12227
Residues n_residues1457
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 dmax136.5
Rg (real space) rg_real40.67
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real3.7150e+08
I(0) uncertainty (real space) i0_real_error6.8190e+06
Rg (reciprocal space) rg_reciprocal40.73
I(0) (reciprocal space) i0_reciprocal371500000.0000
Solution quality estimate total_estimate0.8748
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis-0.140
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35450000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)