9bf0

MID domain of human Argo2 bound to UTP

Method: X-RAY DIFFRACTION Dmax: 92.0 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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 442–575 Chain B; UniProt 442–575 Chain C; UniProt 442–575 Not recorded UTP URIDINE 5'-TRIPHOSPHATE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;drop was 1:1 15 mg/ml protein with RNA: 1.4 M Sodium citrate tribasic dihydrate, 0.1 M HEPES pH 7.5 Resolution 1.78 Å R-free 0.234

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 1–134; UniProt 442–575 Author chain B; PDBConstruct 1–134; UniProt 442–575 Author chain C; PDBConstruct 1–134; UniProt 442–575

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 9bf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bf0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bf0
Deposition date deposition_date2024-04-16
最后修订 last_revision2024-07-10
Structure title titleMID domain of human Argo2 bound to UTP
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_guinier27.79
Radius of gyration Rg (electron density) rg_electron27.27
Forward intensity I(0) i035569000.00
Molecular weight molecular_weight45448.0 kDa
Excluded volume excluded_volume56676 ų
Envelope volume envelope_volume69765 ų
Hydration-shell volume shell_volume22757 ų
Envelope diameter envelope_diameter94.2
Shell Rg shell_rg32.63
Envelope Rg envelope_rg27.12
Shape Rg shape_rg27.29
Total Rg total_rg27.81
Total atoms total_atoms3161
Residues n_residues396
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 dmax92.0
Rg (real space) rg_real27.92
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real3.5570e+07
I(0) uncertainty (real space) i0_real_error5.5440e+05
Rg (reciprocal space) rg_reciprocal27.89
I(0) (reciprocal space) i0_reciprocal35570000.0000
Solution quality estimate total_estimate0.8604
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16480000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.818; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)