7w9m

Cryo-EM structure of human Nav1.7(E406K) in complex with auxiliary beta subunits, ProTx-II and tetrodotoxin (S6IV pi helix conformer)

Method: ELECTRON MICROSCOPY Dmax: 147.8 Å Quality: GOOD

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

Sodium channel protein type 9 subunit alpha

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 Other combination Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1988 Mutation:E406K Sodium channel subunit beta-1 × 1 (Q07699) Sodium channel subunit beta-2 × 1 (O60939) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 9SR (1R,5R,6R,7R,9S,11S,12S,13S,14S)-3-amino-14-(hydroxymethyl)-8,10-dioxa-2,4-diazatetracyclo[7.3.1.1~7,11~.0~1,6~]tetradec-3-ene-5,9,12,13,14-pentol (non-preferred name) × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 5 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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 44–2031; UniProt 1–1988

Sodium channel 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 B; UniProt 1–218 Not recorded Sodium channel protein type 9 subunit alpha × 1 (Q15858) Sodium channel subunit beta-2 × 1 (O60939) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 9SR (1R,5R,6R,7R,9S,11S,12S,13S,14S)-3-amino-14-(hydroxymethyl)-8,10-dioxa-2,4-diazatetracyclo[7.3.1.1~7,11~.0~1,6~]tetradec-3-ene-5,9,12,13,14-pentol (non-preferred name) × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 5 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–218; UniProt 1–218

Sodium channel subunit beta-2

Homo sapiens

UniProt O60939

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 1–215 Not recorded Sodium channel protein type 9 subunit alpha × 1 (Q15858) Sodium channel subunit beta-1 × 1 (Q07699) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 9SR (1R,5R,6R,7R,9S,11S,12S,13S,14S)-3-amino-14-(hydroxymethyl)-8,10-dioxa-2,4-diazatetracyclo[7.3.1.1~7,11~.0~1,6~]tetradec-3-ene-5,9,12,13,14-pentol (non-preferred name) × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 P5S O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine × 1 Y01 CHOLESTEROL HEMISUCCINATE × 5 LPE 1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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

View Construct and Data Evidence
UniProt name SCN2B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–215; UniProt 1–215

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 7w9m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w9m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7w9m
Deposition date deposition_date2021-12-10
Structure title titleCryo-EM structure of human Nav1.7(E406K) in complex with auxiliary beta subunits, ProTx-II and tetrodotoxin (S6IV pi helix conformer)
Keywords keywordsNav1.7, SCN9A, cryo-EM, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.49
Radius of gyration Rg (electron density) rg_electron43.63
Forward intensity I(0) i0515891000.00
Molecular weight molecular_weight202000.0 kDa
Excluded volume excluded_volume259170 ų
Envelope volume envelope_volume376890 ų
Hydration-shell volume shell_volume72155 ų
Envelope diameter envelope_diameter147.4
Shell Rg shell_rg48.14
Envelope Rg envelope_rg43.33
Shape Rg shape_rg43.64
Total Rg total_rg43.84
Total atoms total_atoms14210
Residues n_residues1710
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 dmax147.8
Rg (real space) rg_real44.36
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real5.1590e+08
I(0) uncertainty (real space) i0_real_error9.6240e+06
Rg (reciprocal space) rg_reciprocal44.49
I(0) (reciprocal space) i0_reciprocal516000000.0000
Solution quality estimate total_estimate0.8719
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34250000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)