7zlq

Crystal structure of ADAR1-dsRBD3 dimer in complex with dsRNA

Method: X-RAY DIFFRACTION Dmax: 88.0 Å Quality: GOOD

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

Double-stranded RNA-specific adenosine deaminase

Homo sapiens

UniProt P55265

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 Homooligomer Protein × 2 RNA 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 716–797 Chain B; UniProt 716–797 Not recorded ;RNA (5'-R(*CP*GP*AP*AP*GP*CP*CP*UP*UP*CP*GP*CP*G)-3') ; × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;50 mM sodium cacodylate, 5% (w/v) PEG 4000, 30 mM CaCl2, 230 mM KCl Resolution 2.80 Å R-free 0.266

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.

23 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DSRAD_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–86; UniProt 716–797 Author chain B; PDBConstruct 5–86; UniProt 716–797

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 7zlq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zlq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zlq
Deposition date deposition_date2022-04-15
Structure title titleCrystal structure of ADAR1-dsRBD3 dimer in complex with dsRNA
Keywords keywordsEditing, ADAR, RNA-binding domain, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.26
Radius of gyration Rg (electron density) rg_electron24.19
Forward intensity I(0) i025617000.00
Molecular weight molecular_weight30162.0 kDa
Excluded volume excluded_volume34011 ų
Envelope volume envelope_volume48273 ų
Hydration-shell volume shell_volume18441 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg28.70
Envelope Rg envelope_rg24.32
Shape Rg shape_rg24.03
Total Rg total_rg25.01
Total atoms total_atoms2079
Residues n_residues203
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 dmax88.0
Rg (real space) rg_real26.47
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real2.5620e+07
I(0) uncertainty (real space) i0_real_error4.1860e+05
Rg (reciprocal space) rg_reciprocal26.41
I(0) (reciprocal space) i0_reciprocal25620000.0000
Solution quality estimate total_estimate0.8630
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.441
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1168000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.734; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)