7jl3

Cryo-EM structure of RIG-I:dsRNA filament in complex with RIPLET PrySpry domain (trimer)

Method: ELECTRON MICROSCOPY Dmax: 170.9 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 Heteromer Protein × 6 RNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 159–880 Chain C; UniProt 159–880 Chain E; UniProt 159–880 Fragment:UNP residues 159-880 E3 ubiquitin-protein ligase RNF135 × 3 (Q8IUD6) dsRNA strand1 × 1 dsRNA strand 2 × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ALF TETRAFLUOROALUMINATE ION × 3 MG MAGNESIUM ION × 3 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

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 O95786-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–722; UniProt 159–880 Author chain C; PDBConstruct 1–722; UniProt 159–880 Author chain E; PDBConstruct 1–722; UniProt 159–880

E3 ubiquitin-protein ligase RNF135

Homo sapiens

UniProt Q8IUD6

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 Heteromer Protein × 6 RNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain B; UniProt 249–432 Chain D; UniProt 249–432 Chain F; UniProt 249–432 Fragment:RIPLET PrySpry domain (UNP residues 249-432) Antiviral innate immune response receptor RIG-I × 3 (O95786) dsRNA strand1 × 1 dsRNA strand 2 × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ALF TETRAFLUOROALUMINATE ION × 3 MG MAGNESIUM ION × 3 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN135_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–184; UniProt 249–432 Author chain D; PDBConstruct 1–184; UniProt 249–432 Author chain F; PDBConstruct 1–184; UniProt 249–432

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 7jl3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jl3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jl3
Deposition date deposition_date2020-07-29
Structure title titleCryo-EM structure of RIG-I:dsRNA filament in complex with RIPLET PrySpry domain (trimer)
Keywords keywordsInnate immunity, E3 ligase, helicase, antiviral signaling, RLR, dsRNA sensor, HYDROLASE-TRANSFERASE-RNA complex; HYDROLASE/TRANSFERASE/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.87
Radius of gyration Rg (electron density) rg_electron51.62
Forward intensity I(0) i01464570000.00
Molecular weight molecular_weight303630.0 kDa
Excluded volume excluded_volume373760 ų
Envelope volume envelope_volume566590 ų
Hydration-shell volume shell_volume93131 ų
Envelope diameter envelope_diameter184.1
Shell Rg shell_rg53.35
Envelope Rg envelope_rg50.45
Shape Rg shape_rg51.68
Total Rg total_rg51.51
Total atoms total_atoms21219
Residues n_residues2541
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 dmax170.9
Rg (real space) rg_real50.95
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real1.4650e+09
I(0) uncertainty (real space) i0_real_error2.6000e+07
Rg (reciprocal space) rg_reciprocal50.79
I(0) (reciprocal space) i0_reciprocal1464000000.0000
Solution quality estimate total_estimate0.6374
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.1
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.394
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha131200000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 0.003; Positv: 1.000; Valcen: 0.988; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)