6n4q

CryoEM structure of Nav1.7 VSD2 (actived state) in complex with the gating modifier toxin ProTx2

Method: ELECTRON MICROSCOPY Dmax: 179.6 Å Quality: GOOD

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

Nav1.7 VSD2-NavAb chimera

Arcobacter butzleri (strain RM4018)

UniProt A8EVM5

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–25 Chain A; UniProt 58–78 Chain A; UniProt 107–267 Chain B; UniProt 1–25 Chain B; UniProt 58–78 Chain B; UniProt 107–267 Chain C; UniProt 1–25 Chain C; UniProt 58–78 Chain C; UniProt 107–267 Chain D; UniProt 1–25 Chain D; UniProt 58–78 Chain D; UniProt 107–267 Not recorded Beta/omega-theraphotoxin-Tp2a × 4 (P83476) Fab light chain × 2 Fab heavy chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris pH 8.0, 100 mM NaCl, 0.06% FA3, 0.1 mg/ml POPC:POPE:POPG mixed at molar ratio 3:1:1 cryo-EM vitrification conditions:Cryogen ETHANE;Apply 3 uL, blot 2.5s. Ted Pella 595 filter paper. Resolution 3.60 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.

71 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A8EVM5_ARCB4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–43; UniProt 1–25 Author chain A; PDBConstruct 75–95; UniProt 58–78 Author chain A; PDBConstruct 128–288; UniProt 107–267 Author chain B; PDBConstruct 19–43; UniProt 1–25 Author chain B; PDBConstruct 75–95; UniProt 58–78 Author chain B; PDBConstruct 128–288; UniProt 107–267 Author chain C; PDBConstruct 19–43; UniProt 1–25 Author chain C; PDBConstruct 75–95; UniProt 58–78 Author chain C; PDBConstruct 128–288; UniProt 107–267 Author chain D; PDBConstruct 19–43; UniProt 1–25 Author chain D; PDBConstruct 75–95; UniProt 58–78 Author chain D; PDBConstruct 128–288; UniProt 107–267

Nav1.7 VSD2-NavAb chimera

Arcobacter butzleri (strain RM4018)

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 747–777 Chain A; UniProt 811–842 Chain B; UniProt 747–777 Chain B; UniProt 811–842 Chain C; UniProt 747–777 Chain C; UniProt 811–842 Chain D; UniProt 747–777 Chain D; UniProt 811–842 Not recorded Beta/omega-theraphotoxin-Tp2a × 4 (P83476) Fab light chain × 2 Fab heavy chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris pH 8.0, 100 mM NaCl, 0.06% FA3, 0.1 mg/ml POPC:POPE:POPG mixed at molar ratio 3:1:1 cryo-EM vitrification conditions:Cryogen ETHANE;Apply 3 uL, blot 2.5s. Ted Pella 595 filter paper. Resolution 3.60 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 Q15858-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 44–74; UniProt 747–777 Author chain A; PDBConstruct 96–127; UniProt 811–842 Author chain B; PDBConstruct 44–74; UniProt 747–777 Author chain B; PDBConstruct 96–127; UniProt 811–842 Author chain C; PDBConstruct 44–74; UniProt 747–777 Author chain C; PDBConstruct 96–127; UniProt 811–842 Author chain D; PDBConstruct 44–74; UniProt 747–777 Author chain D; PDBConstruct 96–127; UniProt 811–842

Beta/omega-theraphotoxin-Tp2a

OrganismNot specified

UniProt P83476

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 1–30 Chain F; UniProt 1–30 Chain G; UniProt 1–30 Chain H; UniProt 1–30 Not recorded Nav1.7 VSD2-NavAb chimera × 4 (A8EVM5,Q15858) Fab light chain × 2 Fab heavy chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris pH 8.0, 100 mM NaCl, 0.06% FA3, 0.1 mg/ml POPC:POPE:POPG mixed at molar ratio 3:1:1 cryo-EM vitrification conditions:Cryogen ETHANE;Apply 3 uL, blot 2.5s. Ted Pella 595 filter paper. Resolution 3.60 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TXPR2_THRPR
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–30; UniProt 1–30 Author chain F; PDBConstruct 1–30; UniProt 1–30 Author chain G; PDBConstruct 1–30; UniProt 1–30 Author chain H; PDBConstruct 1–30; UniProt 1–30

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 6n4q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n4q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n4q
Deposition date deposition_date2018-11-20
Structure title titleCryoEM structure of Nav1.7 VSD2 (actived state) in complex with the gating modifier toxin ProTx2
Keywords keywordsvoltage-gated sodium channel, gating modifier toxin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.87
Radius of gyration Rg (electron density) rg_electron49.19
Forward intensity I(0) i0711812000.00
Molecular weight molecular_weight232500.0 kDa
Excluded volume excluded_volume295610 ų
Envelope volume envelope_volume452390 ų
Hydration-shell volume shell_volume78439 ų
Envelope diameter envelope_diameter193.3
Shell Rg shell_rg51.67
Envelope Rg envelope_rg48.80
Shape Rg shape_rg49.15
Total Rg total_rg49.43
Total atoms total_atoms16358
Residues n_residues2052
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 dmax179.6
Rg (real space) rg_real49.99
Rg uncertainty (real space) rg_real_error2.09
I(0) (real space) i0_real7.1180e+08
I(0) uncertainty (real space) i0_real_error1.4040e+07
Rg (reciprocal space) rg_reciprocal49.87
I(0) (reciprocal space) i0_reciprocal711700000.0000
Solution quality estimate total_estimate0.8358
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.7
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis0.259
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43680000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.666; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6n4qI01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6n4qI02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6n4qJ02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6n4qK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6n4qK02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6n4qL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)