3jrv

Structure of poxvirus K7 protein in complex with RNA helicase DDX3

Method: X-RAY DIFFRACTION Dmax: 68.3 Å Quality: GOOD

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

Protein K7

Vaccinia virus WR

UniProt P68466

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–149 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP-dependent RNA helicase DDX3X × 1 (O00571) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.25;291 K;100mM sodium citrate, 15.0% (w/v) PEG 3350, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.60 Å R-free 0.190
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–149 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP-dependent RNA helicase DDX3X × 1 (O00571) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.25;291 K;100mM sodium citrate, 15.0% (w/v) PEG 3350, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.60 Å R-free 0.190

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VK07_VACCW
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–149; UniProt 1–149 Author chain B; PDBConstruct 1–149; UniProt 1–149

ATP-dependent RNA helicase DDX3X

OrganismNot specified

UniProt O00571

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 71–90 Fragment:DDX3, UNP residues 71-90 Protein K7 × 1 (P68466) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.25;291 K;100mM sodium citrate, 15.0% (w/v) PEG 3350, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.60 Å R-free 0.190
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 71–90 Fragment:DDX3, UNP residues 71-90 Protein K7 × 1 (P68466) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.25;291 K;100mM sodium citrate, 15.0% (w/v) PEG 3350, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.60 Å R-free 0.190
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 71–90 Fragment:DDX3, UNP residues 71-90 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.25;291 K;100mM sodium citrate, 15.0% (w/v) PEG 3350, pH 5.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.60 Å R-free 0.190

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.

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDX3X_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 71–90 Author chain D; PDBConstruct 1–20; UniProt 71–90 Author chain E; PDBConstruct 1–20; UniProt 71–90

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 3jrv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jrv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jrv
Deposition date deposition_date2009-09-09
Structure title titleStructure of poxvirus K7 protein in complex with RNA helicase DDX3
Keywords keywordspoxvirus protein K7, DEAD-box RNA Helicase DDX3, viral immune evasion, innate immunity, VIRAL PROTEIN-PROTEIN BINDING complex; VIRAL PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.37
Radius of gyration Rg (electron density) rg_electron20.24
Forward intensity I(0) i021787900.00
Molecular weight molecular_weight35787.0 kDa
Excluded volume excluded_volume44664 ų
Envelope volume envelope_volume51933 ų
Hydration-shell volume shell_volume21491 ų
Envelope diameter envelope_diameter68.2
Shell Rg shell_rg26.62
Envelope Rg envelope_rg20.24
Shape Rg shape_rg20.25
Total Rg total_rg21.05
Total atoms total_atoms2505
Residues n_residues301
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 dmax68.3
Rg (real space) rg_real21.30
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.1790e+07
I(0) uncertainty (real space) i0_real_error2.8520e+05
Rg (reciprocal space) rg_reciprocal21.32
I(0) (reciprocal space) i0_reciprocal21790000.0000
Solution quality estimate total_estimate0.8933
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5827000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3jrvA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily20 — dsDNA poxvirus
Domain ID domain_id3jrvB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily20 — dsDNA poxvirus

8. Citations (1)

9. Files and Curves (10)