2qfb

Crystal structure of the regulatory domain of human RIG-I with bound Zn

Method: X-RAY DIFFRACTION Dmax: 134.8 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 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
10 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain J; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285
9 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 802–925 Fragment:Regulatory domain ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10;293.15 K;0.1 M CHES, 18% w/v PEG 8000, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 3.00 Å R-free 0.285

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 61 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 22–145; UniProt 802–925 Author chain B; PDBConstruct 22–145; UniProt 802–925 Author chain C; PDBConstruct 22–145; UniProt 802–925 Author chain D; PDBConstruct 22–145; UniProt 802–925 Author chain E; PDBConstruct 22–145; UniProt 802–925 Author chain F; PDBConstruct 22–145; UniProt 802–925 Author chain G; PDBConstruct 22–145; UniProt 802–925 Author chain H; PDBConstruct 22–145; UniProt 802–925 Author chain I; PDBConstruct 22–145; UniProt 802–925 Author chain J; PDBConstruct 22–145; 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 2qfb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2qfb
Deposition date deposition_date2007-06-27
Structure title titleCrystal structure of the regulatory domain of human RIG-I with bound Zn
Keywords keywords;Zinc finger, Alternative splicing, Antiviral defense, ATP-binding, Helicase, Hydrolase, Immune response, Innate immunity, Interferon induction, Nucleotide-binding, Polymorphism, RNA-binding, Ubl conjugation ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.14
Radius of gyration Rg (electron density) rg_electron43.64
Forward intensity I(0) i0285276000.00
Molecular weight molecular_weight142470.0 kDa
Excluded volume excluded_volume179980 ų
Envelope volume envelope_volume280910 ų
Hydration-shell volume shell_volume54278 ų
Envelope diameter envelope_diameter139.8
Shell Rg shell_rg49.02
Envelope Rg envelope_rg41.39
Shape Rg shape_rg43.63
Total Rg total_rg43.97
Total atoms total_atoms9990
Residues n_residues1210
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 dmax134.8
Rg (real space) rg_real43.99
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real2.8530e+08
I(0) uncertainty (real space) i0_real_error5.3530e+06
Rg (reciprocal space) rg_reciprocal44.14
I(0) (reciprocal space) i0_reciprocal285300000.0000
Solution quality estimate total_estimate0.8958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.2
Skewness Skewness skewness0.055
Kurtosis Kurtosis kurtosis-0.709
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14980000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.700

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd2qfba_
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_idd2qfbb_
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_idd2qfbc_
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_idd2qfbd_
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_idd2qfbe_
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_idd2qfbf_
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_idd2qfbg_
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_idd2qfbh_
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_idd2qfbi_
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_idd2qfbj_
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 (10 domains)

Domain ID domain_id2qfbA00
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_id2qfbB00
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_id2qfbC00
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_id2qfbD00
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_id2qfbE00
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_id2qfbF00
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_id2qfbG00
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_id2qfbH00
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_id2qfbI00
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_id2qfbJ00
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)