3ews

Human DEAD-box RNA-helicase DDX19 in complex with ADP

Method: X-RAY DIFFRACTION Dmax: 99.8 Å Quality: GOOD

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

ATP-dependent RNA helicase DDX19B

Homo sapiens

UniProt Q9UMR2

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 54–475 Fragment:Helicase ATP-binding domain, Helicase C-terminal domain, UNP residues 54-475 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1M ammonium acetate, 0.1M Bis-Tris, 17% PEG-10000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.70 Å R-free 0.260
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 54–475 Fragment:Helicase ATP-binding domain, Helicase C-terminal domain, UNP residues 54-475 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;0.1M ammonium acetate, 0.1M Bis-Tris, 17% PEG-10000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.70 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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DD19B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–445; UniProt 54–475 Author chain B; PDBConstruct 24–445; UniProt 54–475

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 3ews

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3ews
Deposition date deposition_date2008-10-16
Structure title titleHuman DEAD-box RNA-helicase DDX19 in complex with ADP
Keywords keywords;RNA HELICASE, DEAD, ADP, Structural Genomics, Structural Genomics Consortium, SGC, rRNA, ATP-binding, Hydrolase, Nucleotide-binding, RNA-binding, mRNA, Alternative splicing, Cytoplasm, Helicase, Membrane, mRNA transport, Nuclear pore complex, Nucleus, Protein transport, Translocation, Transport ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.41
Radius of gyration Rg (electron density) rg_electron30.48
Forward intensity I(0) i0136787000.00
Molecular weight molecular_weight92498.0 kDa
Excluded volume excluded_volume115820 ų
Envelope volume envelope_volume147610 ų
Hydration-shell volume shell_volume39625 ų
Envelope diameter envelope_diameter106.6
Shell Rg shell_rg38.31
Envelope Rg envelope_rg30.25
Shape Rg shape_rg30.51
Total Rg total_rg31.06
Total atoms total_atoms6482
Residues n_residues821
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 dmax99.8
Rg (real space) rg_real31.32
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real1.3680e+08
I(0) uncertainty (real space) i0_real_error2.0220e+06
Rg (reciprocal space) rg_reciprocal31.36
I(0) (reciprocal space) i0_reciprocal136800000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary97.8
Skewness Skewness skewness0.237
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94590000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.809

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3ewsA01
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_id3ewsA02
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_id3ewsB01
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_id3ewsB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)