9b83

Cryo-EM structure of human ADAR1 in complex with dsRNA derived from human GLI1 gene

Method: ELECTRON MICROSCOPY Dmax: 101.6 Å Quality: REASONABLE

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

Maltodextrin-binding protein,Double-stranded RNA-specific adenosine deaminase

Homo sapiens

UniProt C3SHQ8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 27–392 Chain B; UniProt 27–392 Not recorded RNA (31-MER) × 1 IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 Å

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.

15 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SHQ8_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392 Author chain B; PDBConstruct 2–367; UniProt 27–392

Maltodextrin-binding protein,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 Insufficient information Homooligomer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 127–1226 Chain B; UniProt 127–1226 Not recorded RNA (31-MER) × 1 IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 Å

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 2
Chains and sequence ranges Author chain A; PDBConstruct 393–1492; UniProt 127–1226 Author chain B; PDBConstruct 393–1492; UniProt 127–1226

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 9b83

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b83
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b83
Deposition date deposition_date2024-03-28
Structure title titleCryo-EM structure of human ADAR1 in complex with dsRNA derived from human GLI1 gene
Keywords keywordsADAR1-dsRNA complex, HYDROLASE-RNA complex; HYDROLASE/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.15
Radius of gyration Rg (electron density) rg_electron30.98
Forward intensity I(0) i0162361000.00
Molecular weight molecular_weight92358.0 kDa
Excluded volume excluded_volume111870 ų
Envelope volume envelope_volume146520 ų
Hydration-shell volume shell_volume39391 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg37.91
Envelope Rg envelope_rg31.03
Shape Rg shape_rg31.03
Total Rg total_rg31.41
Total atoms total_atoms6418
Residues n_residues765
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 dmax101.6
Rg (real space) rg_real31.15
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real1.6240e+08
I(0) uncertainty (real space) i0_real_error2.5420e+06
Rg (reciprocal space) rg_reciprocal31.15
I(0) (reciprocal space) i0_reciprocal162400000.0000
Solution quality estimate total_estimate0.6698
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28290000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 0.040; Positv: 1.000; Valcen: 0.979; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)