7fbs

structure of a channel

Method: ELECTRON MICROSCOPY Dmax: 116.7 Å Quality: GOOD

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

;Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein ;

Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP

UniProt B7UCZ6

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 512–750 Mutation:I1487Q,F1488Q,M1489Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 11 4Y4 1-[2-[(2R)-2-oxidanyl-3-(propylamino)propoxy]phenyl]-3-phenyl-propan-1-one × 1 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 B7UCZ6_9RHAB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1590–1828; UniProt 512–750

;Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein ;

Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP

UniProt P15389

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–461 Chain A; UniProt 659–1068 Chain A; UniProt 1190–1898 Mutation:I1487Q,F1488Q,M1489Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 11 4Y4 1-[2-[(2R)-2-oxidanyl-3-(propylamino)propoxy]phenyl]-3-phenyl-propan-1-one × 1 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 SCN5A_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–461; UniProt 1–461 Author chain A; PDBConstruct 462–871; UniProt 659–1068 Author chain A; PDBConstruct 872–1580; UniProt 1190–1898

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 7fbs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7fbs
Deposition date deposition_date2021-07-12
Structure title titlestructure of a channel
Keywords keywordsion channel, four-domain, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.52
Radius of gyration Rg (electron density) rg_electron34.60
Forward intensity I(0) i0211897000.00
Molecular weight molecular_weight131610.0 kDa
Excluded volume excluded_volume170710 ų
Envelope volume envelope_volume223160 ų
Hydration-shell volume shell_volume53025 ų
Envelope diameter envelope_diameter126.1
Shell Rg shell_rg41.49
Envelope Rg envelope_rg35.27
Shape Rg shape_rg34.62
Total Rg total_rg35.08
Total atoms total_atoms9274
Residues n_residues1118
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 dmax116.7
Rg (real space) rg_real35.40
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real2.1190e+08
I(0) uncertainty (real space) i0_real_error3.7040e+06
Rg (reciprocal space) rg_reciprocal35.48
I(0) (reciprocal space) i0_reciprocal211900000.0000
Solution quality estimate total_estimate0.8821
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.7
Skewness Skewness skewness0.237
Kurtosis Kurtosis kurtosis-0.254
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21080000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7fbsA01
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

8. Citations (1)

9. Files and Curves (10)