7yq6

human insulin receptor bound with A62 DNA aptamer

Method: ELECTRON MICROSCOPY Dmax: 155.7 Å Quality: GOOD

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

Isoform Short of Insulin receptor

Homo sapiens

UniProt P06213

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain E; UniProt 28–934 Chain F; UniProt 28–934 Not recorded IR-A62 aptamer × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

85 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSR_HUMAN
Isoform P06213-2
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–907; UniProt 28–934 Author chain F; PDBConstruct 1–907; UniProt 28–934

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 7yq6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yq6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7yq6
Deposition date deposition_date2022-08-05
Structure title titlehuman insulin receptor bound with A62 DNA aptamer
Keywords keywordsreceptor-ligand complex_C, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.74
Radius of gyration Rg (electron density) rg_electron51.41
Forward intensity I(0) i0653128000.00
Molecular weight molecular_weight199720.0 kDa
Excluded volume excluded_volume244520 ų
Envelope volume envelope_volume424990 ų
Hydration-shell volume shell_volume70478 ų
Envelope diameter envelope_diameter156.8
Shell Rg shell_rg55.70
Envelope Rg envelope_rg47.85
Shape Rg shape_rg51.40
Total Rg total_rg51.62
Total atoms total_atoms13976
Residues n_residues1608
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 dmax155.7
Rg (real space) rg_real51.54
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real6.5310e+08
I(0) uncertainty (real space) i0_real_error1.1930e+07
Rg (reciprocal space) rg_reciprocal51.88
I(0) (reciprocal space) i0_reciprocal653400000.0000
Solution quality estimate total_estimate0.8693
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.7
Skewness Skewness skewness-0.015
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23110000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.362

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)