4pxa

DEAD-box RNA helicase DDX3X Cancer-associated mutant D354V

Method: X-RAY DIFFRACTION Dmax: 78.2 Å Quality: GOOD

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

ATP-dependent RNA helicase DDX3X

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 135–582 Fragment:D1-D2, UNP residues 135-582 Mutation:D354V ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;1.66 M NaH2PO4 0.24 M K2HPO4, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K Resolution 3.20 Å R-free 0.271

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 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDX3X_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–467; UniProt 135–582

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 4pxa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pxa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4pxa
Deposition date deposition_date2014-03-22
Structure title titleDEAD-box RNA helicase DDX3X Cancer-associated mutant D354V
Keywords keywordsDEAD-box helicase, HYDROLASE, TRANSLATION, RNA BINDING PROTEIN; TRANSLATION, RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.61
Radius of gyration Rg (electron density) rg_electron23.60
Forward intensity I(0) i045742100.00
Molecular weight molecular_weight50629.0 kDa
Excluded volume excluded_volume62747 ų
Envelope volume envelope_volume76035 ų
Hydration-shell volume shell_volume26887 ų
Envelope diameter envelope_diameter78.8
Shell Rg shell_rg30.96
Envelope Rg envelope_rg23.82
Shape Rg shape_rg23.64
Total Rg total_rg24.31
Total atoms total_atoms3547
Residues n_residues442
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 dmax78.2
Rg (real space) rg_real24.58
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real4.5740e+07
I(0) uncertainty (real space) i0_real_error6.6240e+05
Rg (reciprocal space) rg_reciprocal24.59
I(0) (reciprocal space) i0_reciprocal45740000.0000
Solution quality estimate total_estimate0.8950
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.349
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12580000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.940

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_id4pxaA01
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_id4pxaA02
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)