3og8

Crystal structure of human RIG-I CTD bound to a 14-bp blunt-ended dsRNA

Method: X-RAY DIFFRACTION Dmax: 93.0 Å Quality: GOOD

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 Homooligomer Protein × 2 RNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 802–925 Chain B; UniProt 802–925 Fragment:C-terminal domain Mutation:C829S ;RNA (5'-R(*GP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*C)-3') ; × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;27% PEG MME 550, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.40 Å R-free 0.278

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 A; PDBConstruct 2–125; UniProt 802–925 Author chain B; PDBConstruct 2–125; UniProt 802–925

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 3og8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3og8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3og8
Deposition date deposition_date2010-08-16
Structure title titleCrystal structure of human RIG-I CTD bound to a 14-bp blunt-ended dsRNA
Keywords keywordsInnate immunity, viral RNA sensing, RNA binding domain, IPS-1, cytosolic, HYDROLASE-RNA complex; HYDROLASE/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.76
Radius of gyration Rg (electron density) rg_electron24.46
Forward intensity I(0) i033284400.00
Molecular weight molecular_weight38936.0 kDa
Excluded volume excluded_volume46180 ų
Envelope volume envelope_volume59837 ų
Hydration-shell volume shell_volume21364 ų
Envelope diameter envelope_diameter93.7
Shell Rg shell_rg30.32
Envelope Rg envelope_rg24.74
Shape Rg shape_rg24.49
Total Rg total_rg24.98
Total atoms total_atoms2696
Residues n_residues282
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 dmax93.0
Rg (real space) rg_real23.94
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real3.3280e+07
I(0) uncertainty (real space) i0_real_error4.9620e+05
Rg (reciprocal space) rg_reciprocal23.90
I(0) (reciprocal space) i0_reciprocal33280000.0000
Solution quality estimate total_estimate0.7575
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis-0.021
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5072000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.440; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.522; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd3og8a1
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_idd3og8a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3og8b1
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_idd3og8b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3og8b3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3og8A00
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_id3og8B00
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)