9b89

Cryo-EM structure of human ADAR1 in complex with dsRNA derived from HT2C gene in the pre-editing state

Method: ELECTRON MICROSCOPY Dmax: 111.7 Å Quality: GOOD

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 (71-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 3.87 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 1
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 (71-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 3.87 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 1
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 9b89

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b89
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b89
Deposition date deposition_date2024-03-29
Structure title titleCryo-EM structure of human ADAR1 in complex with dsRNA derived from HT2C gene in the pre-editing state
Keywords keywordsADAR1-dsRNA complex, pre-editing state, 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_guinier34.61
Radius of gyration Rg (electron density) rg_electron33.61
Forward intensity I(0) i0198957000.00
Molecular weight molecular_weight102830.0 kDa
Excluded volume excluded_volume124540 ų
Envelope volume envelope_volume168600 ų
Hydration-shell volume shell_volume42762 ų
Envelope diameter envelope_diameter111.0
Shell Rg shell_rg39.30
Envelope Rg envelope_rg33.40
Shape Rg shape_rg33.61
Total Rg total_rg34.03
Total atoms total_atoms7148
Residues n_residues852
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 dmax111.7
Rg (real space) rg_real34.56
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real1.9900e+08
I(0) uncertainty (real space) i0_real_error3.4070e+06
Rg (reciprocal space) rg_reciprocal34.60
I(0) (reciprocal space) i0_reciprocal199000000.0000
Solution quality estimate total_estimate0.8318
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.652
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20150000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)