6wuk

Crystal structure of mouse DXO in complex with CoA

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

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

Decapping and exoribonuclease protein

Mus musculus

UniProt O70348

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 1–397 Mutation:E192S/E234Q/E253Q COA COENZYME A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;23% (w/v) PEG3350 Resolution 1.60 Å R-free 0.214

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.

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

View Construct and Data Evidence
UniProt name DXO_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–417; UniProt 1–397

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 6wuk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wuk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wuk
Deposition date deposition_date2020-05-04
Structure title titleCrystal structure of mouse DXO in complex with CoA
Keywords keywordsDXO, decapping, CoA, Coenzyme A, cap, HYDROLASE; HYDROLASE
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_electron20.25
Forward intensity I(0) i030868000.00
Molecular weight molecular_weight41624.0 kDa
Excluded volume excluded_volume51553 ų
Envelope volume envelope_volume60679 ų
Hydration-shell volume shell_volume24376 ų
Envelope diameter envelope_diameter69.6
Shell Rg shell_rg27.36
Envelope Rg envelope_rg20.41
Shape Rg shape_rg20.26
Total Rg total_rg21.08
Total atoms total_atoms2933
Residues n_residues358
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_real21.22
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.0870e+07
I(0) uncertainty (real space) i0_real_error3.8740e+05
Rg (reciprocal space) rg_reciprocal21.25
I(0) (reciprocal space) i0_reciprocal30870000.0000
Solution quality estimate total_estimate0.6930
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.157
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7058000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 0.161; Positv: 1.000; Valcen: 0.992; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)