9ktw

Cryo-EM structure of wild type RIG-I with 5'p-RNA

Method: ELECTRON MICROSCOPY Dmax: 90.0 Å Quality: REASONABLE

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 B; UniProt 1–925 Not recorded ;5'p-RNA (60-MER) ; × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;25mM HEPES, 150mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

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

View Construct and Data Evidence
UniProt name RIGI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; 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 9ktw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ktw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ktw
Deposition date deposition_date2024-12-03
Structure title titleCryo-EM structure of wild type RIG-I with 5'p-RNA
Keywords keywordsRNA recognition, ATP hydrolysis, RLR signaling, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.01
Radius of gyration Rg (electron density) rg_electron28.70
Forward intensity I(0) i0153245000.00
Molecular weight molecular_weight89852.0 kDa
Excluded volume excluded_volume109160 ų
Envelope volume envelope_volume144680 ų
Hydration-shell volume shell_volume41048 ų
Envelope diameter envelope_diameter95.5
Shell Rg shell_rg36.85
Envelope Rg envelope_rg28.35
Shape Rg shape_rg28.73
Total Rg total_rg29.36
Total atoms total_atoms6254
Residues n_residues714
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 dmax90.0
Rg (real space) rg_real28.88
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.5320e+08
I(0) uncertainty (real space) i0_real_error1.9830e+06
Rg (reciprocal space) rg_reciprocal28.94
I(0) (reciprocal space) i0_reciprocal153300000.0000
Solution quality estimate total_estimate0.7080
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24470000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 0.156; Positv: 1.000; Valcen: 0.992; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)