3g0h

Human dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA

Method: X-RAY DIFFRACTION Dmax: 67.8 Å Quality: EXCELLENT

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 54–475 Fragment:UNP residues 54-275 5'-R(P*UP*UP*UP*UP*UP*UP*U)-3' × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8;277 K;14% PEGMME 2000, 0.25M trimethylamine n-oxide, 0.1 M Tris, pH 8, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.275

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 14 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 3–424; 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 3g0h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3g0h
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3g0h
Deposition date deposition_date2009-01-28
Structure title titleHuman dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA
Keywords keywords;PROTEIN-RNA COMPLEX, DBP5, Structural Genomics, Structural Genomics Consortium, SGC, ATP-binding, Helicase, Hydrolase, Membrane, mRNA transport, Nuclear pore complex, Nucleotide-binding, Nucleus, Phosphoprotein, Protein transport, RNA-binding, Translocation, Transport, polyURACIL, HYDROLASE-RNA COMPLEX ;; HYDROLASE/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.18
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i041720700.00
Molecular weight molecular_weight48537.0 kDa
Excluded volume excluded_volume60187 ų
Envelope volume envelope_volume70195 ų
Hydration-shell volume shell_volume26617 ų
Envelope diameter envelope_diameter69.9
Shell Rg shell_rg28.72
Envelope Rg envelope_rg21.54
Shape Rg shape_rg21.31
Total Rg total_rg22.11
Total atoms total_atoms3388
Residues n_residues415
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 dmax67.8
Rg (real space) rg_real22.04
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real4.1720e+07
I(0) uncertainty (real space) i0_real_error4.9400e+05
Rg (reciprocal space) rg_reciprocal22.07
I(0) (reciprocal space) i0_reciprocal41720000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11950000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3g0ha1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd3g0ha2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id3g0hA01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2170
Domain ID domain_id3g0hA02
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_id3g0hA03
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)