6gpg

Structure of the RIG-I Singleton-Merten syndrome variant C268F

Method: X-RAY DIFFRACTION Dmax: 88.7 Å Quality: EXCELLENT

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 Monomer Protein × 1 RNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 232–925 Mutation:C268F ;RNA (5'-R(*CP*GP*AP*CP*GP*CP*UP*AP*GP*CP*GP*UP*CP*G)-3') ; × 2 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;0.1 M MOPS pH 7.5, 17.5 % (w/v) PEG 3350, 0.25 M NaSCN, 3 % (v/v) 2,2,2 trifluoroethanol Resolution 2.89 Å R-free 0.260

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 2
Chains and sequence ranges Author chain A; PDBConstruct 21–714; 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 6gpg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6gpg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6gpg
Deposition date deposition_date2018-06-05
Structure title titleStructure of the RIG-I Singleton-Merten syndrome variant C268F
Keywords keywordsinnate immune system, RIG-I, Singleton-Merten syndrome, RNA-dependent ATPase, RNA binding protein, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.16
Radius of gyration Rg (electron density) rg_electron27.78
Forward intensity I(0) i0124024000.00
Molecular weight molecular_weight83191.0 kDa
Excluded volume excluded_volume102300 ų
Envelope volume envelope_volume131190 ų
Hydration-shell volume shell_volume38470 ų
Envelope diameter envelope_diameter92.4
Shell Rg shell_rg35.95
Envelope Rg envelope_rg27.52
Shape Rg shape_rg27.81
Total Rg total_rg28.48
Total atoms total_atoms5812
Residues n_residues677
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 dmax88.7
Rg (real space) rg_real28.03
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.2400e+08
I(0) uncertainty (real space) i0_real_error1.7770e+06
Rg (reciprocal space) rg_reciprocal28.07
I(0) (reciprocal space) i0_reciprocal124000000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27510000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6gpgA01
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_id6gpgA02
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_id6gpgA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1320 — phosphoenolpyruvate carboxylase, domain 3
Homologous superfamily homologous superfamily30
Domain ID domain_id6gpgA04
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)