10be

Human AGO2 bound to a miR-20a guide and a position 10-11 mismatched target

Method: ELECTRON MICROSCOPY Dmax: 99.8 Å Quality: GOOD

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

Protein argonaute-2

Homo sapiens

UniProt Q9UKV8

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 Monomer Protein × 1 RNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–859 Not recorded Guide RNA × 1 Target RNA × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.02 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.

66 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AGO2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 15–873; UniProt 1–859

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 10be

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10be
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id10be
Deposition date deposition_date2026-01-09
Structure title titleHuman AGO2 bound to a miR-20a guide and a position 10-11 mismatched target
Keywords keywordsComplex, RISC, RNAi, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.92
Radius of gyration Rg (electron density) rg_electron30.90
Forward intensity I(0) i0157885000.00
Molecular weight molecular_weight96472.0 kDa
Excluded volume excluded_volume119360 ų
Envelope volume envelope_volume157350 ų
Hydration-shell volume shell_volume42106 ų
Envelope diameter envelope_diameter105.7
Shell Rg shell_rg38.22
Envelope Rg envelope_rg31.05
Shape Rg shape_rg30.90
Total Rg total_rg31.50
Total atoms total_atoms6757
Residues n_residues811
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 dmax99.8
Rg (real space) rg_real30.90
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.5790e+08
I(0) uncertainty (real space) i0_real_error2.6980e+06
Rg (reciprocal space) rg_reciprocal30.91
I(0) (reciprocal space) i0_reciprocal157900000.0000
Solution quality estimate total_estimate0.8921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.2
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-0.386
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38410000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)