6p6w

Cryo-EM structure of voltage-gated sodium channel NavAb N49K/L109A/M116V/G94C/Q150C disulfide crosslinked mutant in the resting state

Method: ELECTRON MICROSCOPY Dmax: 107.8 Å Quality: GOOD

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

Fusion of Maltose-binding protein and voltage-gated sodium channel NavAb

Arcobacter butzleri (strain RM4018)

UniProt A0A028ANC5

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 Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–392 Chain B; UniProt 1–392 Chain C; UniProt 1–392 Chain D; UniProt 1–392 Mutation:R4A, N49K, L109A, M116V, G94C, Q150C,R4A, N49K, L109A, M116V, G94C, Q150C No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A028ANC5_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–392; UniProt 1–392 Author chain B; PDBConstruct 1–392; UniProt 1–392 Author chain C; PDBConstruct 1–392; UniProt 1–392 Author chain D; PDBConstruct 1–392; UniProt 1–392

Fusion of Maltose-binding protein and voltage-gated sodium channel NavAb

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 Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–267 Chain B; UniProt 1–267 Chain C; UniProt 1–267 Chain D; UniProt 1–267 Mutation:R4A, N49K, L109A, M116V, G94C, Q150C,R4A, N49K, L109A, M116V, G94C, Q150C No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

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 395–661; UniProt 1–267 Author chain B; PDBConstruct 395–661; UniProt 1–267 Author chain C; PDBConstruct 395–661; UniProt 1–267 Author chain D; PDBConstruct 395–661; UniProt 1–267

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 6p6w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6p6w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6p6w
Deposition date deposition_date2019-06-04
Structure title titleCryo-EM structure of voltage-gated sodium channel NavAb N49K/L109A/M116V/G94C/Q150C disulfide crosslinked mutant in the resting state
Keywords keywordsIon channel, ion transport protein, MEMBRANE PROTEIN, metal transport; membrane protein, metal transport
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.71
Radius of gyration Rg (electron density) rg_electron32.99
Forward intensity I(0) i0127074000.00
Molecular weight molecular_weight105690.0 kDa
Excluded volume excluded_volume138900 ų
Envelope volume envelope_volume186620 ų
Hydration-shell volume shell_volume47342 ų
Envelope diameter envelope_diameter115.6
Shell Rg shell_rg39.75
Envelope Rg envelope_rg32.96
Shape Rg shape_rg32.99
Total Rg total_rg33.64
Total atoms total_atoms7468
Residues n_residues916
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 dmax107.8
Rg (real space) rg_real33.58
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.2710e+08
I(0) uncertainty (real space) i0_real_error2.2530e+06
Rg (reciprocal space) rg_reciprocal33.67
I(0) (reciprocal space) i0_reciprocal127100000.0000
Solution quality estimate total_estimate0.8697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.9
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.217
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19950000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.879

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)