6w6o

NaChBac-Nav1.7VSDII chimera and HWTX-IV complex

Method: ELECTRON MICROSCOPY Dmax: 130.7 Å Quality: REASONABLE

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

NaChBac-Nav1.7VSDII chimera

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 817–832 Chain D; UniProt 817–832 Chain F; UniProt 817–832 Chain H; UniProt 817–832 Not recorded Huwentoxin-IV × 4 (P83303) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 10 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 5 seconds before plunging Resolution 3.20 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 98–113; UniProt 817–832 Author chain D; PDBConstruct 98–113; UniProt 817–832 Author chain F; PDBConstruct 98–113; UniProt 817–832 Author chain H; PDBConstruct 98–113; UniProt 817–832

NaChBac-Nav1.7VSDII chimera

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)

UniProt Q9KCR8

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–97 Chain A; UniProt 111–274 Chain D; UniProt 1–97 Chain D; UniProt 111–274 Chain F; UniProt 1–97 Chain F; UniProt 111–274 Chain H; UniProt 1–97 Chain H; UniProt 111–274 Not recorded Huwentoxin-IV × 4 (P83303) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 10 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 5 seconds before plunging Resolution 3.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9KCR8_BACHD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 1–97 Author chain A; PDBConstruct 114–277; UniProt 111–274 Author chain D; PDBConstruct 1–97; UniProt 1–97 Author chain D; PDBConstruct 114–277; UniProt 111–274 Author chain F; PDBConstruct 1–97; UniProt 1–97 Author chain F; PDBConstruct 114–277; UniProt 111–274 Author chain H; PDBConstruct 1–97; UniProt 1–97 Author chain H; PDBConstruct 114–277; UniProt 111–274

Huwentoxin-IV

OrganismNot specified

UniProt P83303

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 53–87 Chain E; UniProt 53–87 Chain G; UniProt 53–87 Chain I; UniProt 53–87 Fragment:UNP residues 53-87 NaChBac-Nav1.7VSDII chimera × 4 (Q9KCR8,Q15858) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 10 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 5 seconds before plunging Resolution 3.20 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TXH4_CYRSC
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–35; UniProt 53–87 Author chain E; PDBConstruct 1–35; UniProt 53–87 Author chain G; PDBConstruct 1–35; UniProt 53–87 Author chain I; PDBConstruct 1–35; UniProt 53–87

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 6w6o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6w6o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6w6o
Deposition date deposition_date2020-03-17
Structure title titleNaChBac-Nav1.7VSDII chimera and HWTX-IV complex
Keywords keywordsNaChBac, Channels, Sodium Ion-Selective, TRANSPORT PROTEIN-TOXIN complex; TRANSPORT PROTEIN/TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.34
Radius of gyration Rg (electron density) rg_electron37.30
Forward intensity I(0) i0182170000.00
Molecular weight molecular_weight130140.0 kDa
Excluded volume excluded_volume171880 ų
Envelope volume envelope_volume224780 ų
Hydration-shell volume shell_volume51265 ų
Envelope diameter envelope_diameter141.9
Shell Rg shell_rg42.17
Envelope Rg envelope_rg37.76
Shape Rg shape_rg37.22
Total Rg total_rg38.04
Total atoms total_atoms9180
Residues n_residues1044
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 dmax130.7
Rg (real space) rg_real39.28
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.8220e+08
I(0) uncertainty (real space) i0_real_error3.2020e+06
Rg (reciprocal space) rg_reciprocal39.32
I(0) (reciprocal space) i0_reciprocal182200000.0000
Solution quality estimate total_estimate0.6514
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.0
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.234
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10150000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 1.000; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6w6oA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily350 — Voltage-gated potassium channels. Chain C
Domain ID domain_id6w6oA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id6w6oD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily350 — Voltage-gated potassium channels. Chain C
Domain ID domain_id6w6oD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id6w6oF01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily350 — Voltage-gated potassium channels. Chain C
Domain ID domain_id6w6oF02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id6w6oH01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily350 — Voltage-gated potassium channels. Chain C
Domain ID domain_id6w6oH02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70

8. Citations (1)

9. Files and Curves (10)