9k6s

Cryo-EM Structure of hAGO2D669A-siRNA-target (19-nt)

Method: ELECTRON MICROSCOPY Dmax: 82.9 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 Mutation:D669A ;RNA (5'-R(P*UP*AP*CP*AP*AP*GP*AP*GP*CP*CP*UP*UP*UP*CP*UP*GP*UP*UP*G)-3') ; × 1 ;RNA (5'-R(P*CP*AP*AP*CP*AP*GP*AP*AP*AP*GP*GP*CP*UP*CP*UP*UP*GP*UP*U)-3') ; × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–859; 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 9k6s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9k6s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9k6s
Deposition date deposition_date2024-10-22
最后修订 last_revision2025-06-25
Structure title titleCryo-EM Structure of hAGO2D669A-siRNA-target (19-nt)
Keywords keywordsArgonaute protein, siRNA, RNA BINDING PROTEIN/RNA, 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_guinier24.15
Radius of gyration Rg (electron density) rg_electron22.89
Forward intensity I(0) i075512300.00
Molecular weight molecular_weight59595.0 kDa
Excluded volume excluded_volume70996 ų
Envelope volume envelope_volume87539 ų
Hydration-shell volume shell_volume30788 ų
Envelope diameter envelope_diameter81.2
Shell Rg shell_rg30.87
Envelope Rg envelope_rg23.23
Shape Rg shape_rg22.85
Total Rg total_rg23.80
Total atoms total_atoms4138
Residues n_residues459
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 dmax82.9
Rg (real space) rg_real24.02
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real7.5510e+07
I(0) uncertainty (real space) i0_real_error1.0930e+06
Rg (reciprocal space) rg_reciprocal24.05
I(0) (reciprocal space) i0_reciprocal75510000.0000
Solution quality estimate total_estimate0.7847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.253
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16430000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; 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)