5f98

Crystal structure of RIG-I in complex with Cap-0 RNA

Method: X-RAY DIFFRACTION Dmax: 198.7 Å Quality: GOOD

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

Probable ATP-dependent RNA helicase DDX58

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 × 6 RNA 6 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 232–925 Chain C; UniProt 232–925 Chain E; UniProt 232–925 Chain G; UniProt 232–925 Chain I; UniProt 232–925 Chain K; UniProt 232–925 Not recorded ;RNA (5'-R(P*GP*AP*AP*UP*AP*UP*AP*AP*UP*AP*GP*UP*GP*AP*UP*AP*UP*UP*AP*UP*AP*UP*UP*C)-3') ; × 6 ZN ZINC ION × 6 MG MAGNESIUM ION × 6 M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;293 K;20% (w/v) PEG 3350, 0.2 M NaSCN, 100 mM MOPS (pH 7.8), 3.5% (v/v) 2,2,2-trifluoroethanol Resolution 3.28 Å R-free 0.277

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 2–695; UniProt 232–925 Author chain C; PDBConstruct 2–695; UniProt 232–925 Author chain E; PDBConstruct 2–695; UniProt 232–925 Author chain G; PDBConstruct 2–695; UniProt 232–925 Author chain I; PDBConstruct 2–695; UniProt 232–925 Author chain K; PDBConstruct 2–695; UniProt 232–925

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 5f98

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5f98
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5f98
Deposition date deposition_date2015-12-09
Structure title titleCrystal structure of RIG-I in complex with Cap-0 RNA
Keywords keywordsComplex, RIG-I, capped RNA, self versus non-self, innate immunity, 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_guinier59.30
Radius of gyration Rg (electron density) rg_electron58.75
Forward intensity I(0) i03528970000.00
Molecular weight molecular_weight468000.0 kDa
Excluded volume excluded_volume571300 ų
Envelope volume envelope_volume885810 ų
Hydration-shell volume shell_volume123400 ų
Envelope diameter envelope_diameter196.4
Shell Rg shell_rg63.82
Envelope Rg envelope_rg56.78
Shape Rg shape_rg58.77
Total Rg total_rg58.80
Total atoms total_atoms32708
Residues n_residues4021
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 dmax198.7
Rg (real space) rg_real59.07
Rg uncertainty (real space) rg_real_error2.14
I(0) (real space) i0_real3.5290e+09
I(0) uncertainty (real space) i0_real_error8.1590e+07
Rg (reciprocal space) rg_reciprocal59.47
I(0) (reciprocal space) i0_reciprocal3531000000.0000
Solution quality estimate total_estimate0.8720
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary76.4
Skewness Skewness skewness0.151
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha186400000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 24 domains

CATH v4.4 (24 domains)

Domain ID domain_id5f98A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98A03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98A04
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_id5f98C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98C02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98C03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98C04
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_id5f98E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98E02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98E03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98E04
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_id5f98G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98G02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98G03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98G04
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_id5f98I01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98I02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98I03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98I04
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_id5f98K01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98K02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5f98K03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id5f98K04
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)