3ncu

Structural and functional insights into pattern recognition by the innate immune receptor RIG-I

Method: X-RAY DIFFRACTION Dmax: 76.5 Å Quality: GOOD

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

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 Homooligomer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 792–925 Chain B; UniProt 792–925 Fragment:residues 792-925 5'-R(*(GDP)P*AP*CP*GP*CP*UP*AP*GP*CP*GP*UP*C)-3' × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;27% (v/v) polyethylene glycerol 3350 (PEG 3350), 50 mM Tris-HCl, pH 7.5, 0.1 M KCl, and 10 mM MgCl2 , VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.55 Å R-free 0.229

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 1–134; UniProt 792–925 Author chain B; PDBConstruct 1–134; UniProt 792–925

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 3ncu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ncu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ncu
Deposition date deposition_date2010-06-05
Structure title titleStructural and functional insights into pattern recognition by the innate immune receptor RIG-I
Keywords keywordsinnate immune receptor, RIG-I c-terminal domain, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.03
Radius of gyration Rg (electron density) rg_electron23.35
Forward intensity I(0) i028786300.00
Molecular weight molecular_weight36198.0 kDa
Excluded volume excluded_volume42986 ų
Envelope volume envelope_volume55129 ų
Hydration-shell volume shell_volume20290 ų
Envelope diameter envelope_diameter80.3
Shell Rg shell_rg29.63
Envelope Rg envelope_rg23.15
Shape Rg shape_rg23.37
Total Rg total_rg23.99
Total atoms total_atoms2502
Residues n_residues262
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 dmax76.5
Rg (real space) rg_real23.08
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.8790e+07
I(0) uncertainty (real space) i0_real_error4.2900e+05
Rg (reciprocal space) rg_reciprocal23.07
I(0) (reciprocal space) i0_reciprocal28790000.0000
Solution quality estimate total_estimate0.8108
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3238000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3ncua_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like
Domain ID domain_idd3ncub_
Class classb — All beta proteins
Fold Fold foldb.88 — Mss4-like
Superfamily Superfamily superfamilyb.88.2 — RIG-I C-terminal-like
Family Family familyb.88.2.1 — RIG-I C-terminal domain-like

CATH v4.4 (2 domains)

Domain ID domain_id3ncuA00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain
Domain ID domain_id3ncuB00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology150 — Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A
Homologous superfamily homologous superfamily30 — RIG-I-like receptor, C-terminal regulatory domain

8. Citations (1)

9. Files and Curves (10)