9dhx

human Argonaute2 R315V/H316A - guide RNA in complex with a fully complementary target

Method: ELECTRON MICROSCOPY Dmax: 96.1 Å Quality: GOOD

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

Argonaute2 R315V/H316A

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:R315V, H316A, S387D, S824A, S828D, S831D, S834A guide RNA × 1 target RNA × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 9dhx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dhx
Deposition date deposition_date2024-09-04
Structure title titlehuman Argonaute2 R315V/H316A - guide RNA in complex with a fully complementary target
Keywords keywordsRNA binding protein, RNP, RNA, Argonaute2, Ago2; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.47
Radius of gyration Rg (electron density) rg_electron28.51
Forward intensity I(0) i0157532000.00
Molecular weight molecular_weight90621.0 kDa
Excluded volume excluded_volume109600 ų
Envelope volume envelope_volume139300 ų
Hydration-shell volume shell_volume40244 ų
Envelope diameter envelope_diameter103.3
Shell Rg shell_rg36.19
Envelope Rg envelope_rg28.68
Shape Rg shape_rg28.50
Total Rg total_rg29.15
Total atoms total_atoms6316
Residues n_residues725
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 dmax96.1
Rg (real space) rg_real28.47
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.5750e+08
I(0) uncertainty (real space) i0_real_error2.5870e+06
Rg (reciprocal space) rg_reciprocal28.47
I(0) (reciprocal space) i0_reciprocal157500000.0000
Solution quality estimate total_estimate0.8305
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.036
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42940000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.516

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)