2lwe

Solution structure of mutant (T170E) second CARD of human RIG-I

Method: SOLUTION NMR Dmax: 38.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 95–190 Fragment:CARD 2 domain Mutation:T170E No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 250;Pressure ambient NMR sample composition:300 uM [U-100% 15N] card2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:300 uM [U-100% 13C; U-100% 15N] card2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:300 uM [U-100% 13C; U-100% 15N] card2, 100% D2O | 100% D2O Resolution not provided

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 5–100; UniProt 95–190

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 2lwe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lwe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lwe
Deposition date deposition_date2012-07-27
Structure title titleSolution structure of mutant (T170E) second CARD of human RIG-I
Keywords keywordsRIG-I, CARD, SENSOR, VIRAL RNA, HELICASE, PHOSPHOMEMETIC MUTANT, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.83
Radius of gyration Rg (electron density) rg_electron12.65
Forward intensity I(0) i0657188000.00
Molecular weight molecular_weight227570.0 kDa
Excluded volume excluded_volume289680 ų
Envelope volume envelope_volume20991 ų
Hydration-shell volume shell_volume12660 ų
Envelope diameter envelope_diameter48.5
Shell Rg shell_rg20.02
Envelope Rg envelope_rg14.49
Shape Rg shape_rg12.59
Total Rg total_rg13.02
Total atoms total_atoms29440
Residues n_residues1920
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 dmax38.4
Rg (real space) rg_real12.75
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real6.5720e+08
I(0) uncertainty (real space) i0_real_error6.9990e+06
Rg (reciprocal space) rg_reciprocal12.76
I(0) (reciprocal space) i0_reciprocal657200000.0000
Solution quality estimate total_estimate0.8211
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.5
Skewness Skewness skewness0.132
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha144200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.061

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lweA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas

8. Citations (1)

9. Files and Curves (10)