8gz2

Cryo-EM structure of human NaV1.6/beta1/beta2-4,9-anhydro-tetrodotoxin

Method: ELECTRON MICROSCOPY Dmax: 138.4 Å Quality: GOOD

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

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 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–218 Not recorded Sodium channel protein type 8 subunit alpha × 1 (Q9UQD0) Sodium channel subunit beta-2 × 1 (O60939) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WMK (1R,2S,3S,4R,5R,9S,11S,12S,14R)-7-amino-2,4,12-trihydroxy-2-(hydroxymethyl)-10,13,15-trioxa-6,8-diazapentacyclo[7.4.1.1~3,12~.0~5,11~.0~5,14~]pentadec-7-en-8-ium (non-preferred name) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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

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 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–1980 Not recorded Sodium channel subunit beta-1 × 1 (Q07699) Sodium channel subunit beta-2 × 1 (O60939) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WMK (1R,2S,3S,4R,5R,9S,11S,12S,14R)-7-amino-2,4,12-trihydroxy-2-(hydroxymethyl)-10,13,15-trioxa-6,8-diazapentacyclo[7.4.1.1~3,12~.0~5,11~.0~5,14~]pentadec-7-en-8-ium (non-preferred name) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1980; UniProt 1–1980

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 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–215 Not recorded Sodium channel subunit beta-1 × 1 (Q07699) Sodium channel protein type 8 subunit alpha × 1 (Q9UQD0) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 WMK (1R,2S,3S,4R,5R,9S,11S,12S,14R)-7-amino-2,4,12-trihydroxy-2-(hydroxymethyl)-10,13,15-trioxa-6,8-diazapentacyclo[7.4.1.1~3,12~.0~5,11~.0~5,14~]pentadec-7-en-8-ium (non-preferred name) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 8gz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8gz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8gz2
Deposition date deposition_date2022-09-24
Structure title titleCryo-EM structure of human NaV1.6/beta1/beta2-4,9-anhydro-tetrodotoxin
Keywords keywordsion channal, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.25
Radius of gyration Rg (electron density) rg_electron39.82
Forward intensity I(0) i0378256000.00
Molecular weight molecular_weight170310.0 kDa
Excluded volume excluded_volume217750 ų
Envelope volume envelope_volume303850 ų
Hydration-shell volume shell_volume63261 ų
Envelope diameter envelope_diameter145.7
Shell Rg shell_rg45.36
Envelope Rg envelope_rg40.26
Shape Rg shape_rg39.83
Total Rg total_rg40.11
Total atoms total_atoms11984
Residues n_residues1467
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 dmax138.4
Rg (real space) rg_real40.16
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real3.7830e+08
I(0) uncertainty (real space) i0_real_error6.7580e+06
Rg (reciprocal space) rg_reciprocal40.25
I(0) (reciprocal space) i0_reciprocal378300000.0000
Solution quality estimate total_estimate0.8660
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.7
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.217
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32280000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.771; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)