9cmp

Structure of human Argonaute2-guide-target complex in a fully paired, slicing-competent conformation

Method: ELECTRON MICROSCOPY Dmax: 98.5 Å Quality: REASONABLE

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 2–859 Mutation:D669A ;RNA (5'-R(P*UP*GP*GP*AP*AP*GP*AP*CP*UP*AP*GP*UP*GP*AP*UP*UP*UP*UP*GP*UP*U)-3') ; × 1 ;RNA (5'-R(*CP*AP*AP*CP*AP*AP*AP*AP*UP*CP*AP*CP*UP*AP*GP*UP*CP*UP*UP*CP*CP*A)-3') ; × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 3–860; UniProt 2–859

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 9cmp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cmp
Deposition date deposition_date2024-07-15
Structure title titleStructure of human Argonaute2-guide-target complex in a fully paired, slicing-competent conformation
Keywords keywordsRNAi, Argonaute, Slicing, 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_guinier30.38
Radius of gyration Rg (electron density) rg_electron30.05
Forward intensity I(0) i0169579000.00
Molecular weight molecular_weight88842.0 kDa
Excluded volume excluded_volume104880 ų
Envelope volume envelope_volume153470 ų
Hydration-shell volume shell_volume41908 ų
Envelope diameter envelope_diameter102.9
Shell Rg shell_rg37.62
Envelope Rg envelope_rg30.59
Shape Rg shape_rg30.14
Total Rg total_rg30.44
Total atoms total_atoms6211
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 dmax98.5
Rg (real space) rg_real30.33
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.6960e+08
I(0) uncertainty (real space) i0_real_error2.5220e+06
Rg (reciprocal space) rg_reciprocal30.35
I(0) (reciprocal space) i0_reciprocal169600000.0000
Solution quality estimate total_estimate0.6950
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.324
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25940000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 1.000; Smooth: 0.826

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)