9bez

MID domain of human Argo2 bound to RNA

Method: X-RAY DIFFRACTION Dmax: 80.7 Å Quality: EXCELLENT

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 440–575 Chain B; UniProt 440–575 Chain C; UniProt 440–575 Not recorded A1ANT [(3~{S},4~{R},5~{R})-5-[5-methyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-4-oxidanyl-oxolan-3-yl] [oxidanyl(phosphonooxy)phosphoryl] hydrogen phosphate × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;Drops were equal volumes of 15 mg/ml protein and 2.1M DL-Malic acid. The reservoir was 2.1M DL-Malic acid. Using MRC drop plates. Resolution 1.90 Å R-free 0.288

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 1–136; UniProt 440–575 Author chain B; PDBConstruct 1–136; UniProt 440–575 Author chain C; PDBConstruct 1–136; UniProt 440–575

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 9bez

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bez
Deposition date deposition_date2024-04-16
最后修订 last_revision2024-07-10
Structure title titleMID domain of human Argo2 bound to RNA
Keywords keywordsMID domain, Argonaute2, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.23
Radius of gyration Rg (electron density) rg_electron24.39
Forward intensity I(0) i036723800.00
Molecular weight molecular_weight45983.0 kDa
Excluded volume excluded_volume57432 ų
Envelope volume envelope_volume70599 ų
Hydration-shell volume shell_volume24758 ų
Envelope diameter envelope_diameter83.0
Shell Rg shell_rg30.86
Envelope Rg envelope_rg24.30
Shape Rg shape_rg24.40
Total Rg total_rg25.12
Total atoms total_atoms3199
Residues n_residues400
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 dmax80.7
Rg (real space) rg_real25.17
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.6720e+07
I(0) uncertainty (real space) i0_real_error5.2630e+05
Rg (reciprocal space) rg_reciprocal25.19
I(0) (reciprocal space) i0_reciprocal36720000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.625
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11370000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)