8sd0

Cryo-EM structure of RIG-I in complex with p3SLR14

Method: ELECTRON MICROSCOPY Dmax: 89.2 Å Quality: EXCELLENT

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

Antiviral innate immune response receptor RIG-I

Homo sapiens

UniProt O95786

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 1–925 Not recorded p3SLR14 × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

43 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDX58_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–925; UniProt 1–925

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 8sd0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sd0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sd0
Deposition date deposition_date2023-04-06
Structure title titleCryo-EM structure of RIG-I in complex with p3SLR14
Keywords keywordsribonucleoprotein complex, RNA sensor, RIG-I like receptor, IMMUNE SYSTEM, IMMUNE SYSTEM-RNA complex; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.56
Radius of gyration Rg (electron density) rg_electron28.12
Forward intensity I(0) i0130493000.00
Molecular weight molecular_weight83648.0 kDa
Excluded volume excluded_volume102120 ų
Envelope volume envelope_volume136600 ų
Hydration-shell volume shell_volume39585 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg36.28
Envelope Rg envelope_rg27.74
Shape Rg shape_rg28.15
Total Rg total_rg28.82
Total atoms total_atoms5829
Residues n_residues667
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 dmax89.2
Rg (real space) rg_real28.38
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.3050e+08
I(0) uncertainty (real space) i0_real_error1.7840e+06
Rg (reciprocal space) rg_reciprocal28.44
I(0) (reciprocal space) i0_reciprocal130500000.0000
Solution quality estimate total_estimate0.9031
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22600000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)