2rmj

Solution structure of RIG-I C-terminal domain

Method: SOLUTION NMR Dmax: 64.1 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 792–925 Fragment:C-terminal domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;288 K;Ionic strength (raw mmCIF value) 0.25 NMR sample composition:0.5mM [U-100% 13C; U-100% 15N] RIG-I, 90% H2O/10% D2O | 90% H2O/10% 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 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 2rmj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rmj
Deposition date deposition_date2007-10-23
Structure title titleSolution structure of RIG-I C-terminal domain
Keywords keywords;RNA binding protein, Alternative splicing, Antiviral defense, ATP-binding, Cytoplasm, Helicase, Hydrolase, Immune response, Innate immunity, Interferon induction, Nucleotide-binding, Polymorphism, RNA-binding, Ubl conjugation ;; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.15
Radius of gyration Rg (electron density) rg_electron15.84
Forward intensity I(0) i01268880000.00
Molecular weight molecular_weight312360.0 kDa
Excluded volume excluded_volume394870 ų
Envelope volume envelope_volume53495 ų
Hydration-shell volume shell_volume21844 ų
Envelope diameter envelope_diameter69.6
Shell Rg shell_rg27.53
Envelope Rg envelope_rg21.32
Shape Rg shape_rg15.81
Total Rg total_rg16.21
Total atoms total_atoms43860
Residues n_residues2680
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 dmax64.1
Rg (real space) rg_real16.17
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.2690e+09
I(0) uncertainty (real space) i0_real_error1.9050e+07
Rg (reciprocal space) rg_reciprocal16.17
I(0) (reciprocal space) i0_reciprocal1269000000.0000
Solution quality estimate total_estimate0.7559
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis0.331
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1018000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.365; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.729; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2rmja_
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 (1 domains)

Domain ID domain_id2rmjA00
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)