9jfd

Human insulin receptor bound with A62-dimer, Pseudo-gamma conformation

Method: ELECTRON MICROSCOPY Dmax: 153.3 Å Quality: GOOD

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

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 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 28–946 Chain B; UniProt 28–946 Not recorded A62 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.35 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
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–919; UniProt 28–946 Author chain B; PDBConstruct 1–919; UniProt 28–946

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 9jfd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9jfd
Deposition date deposition_date2024-09-04
Structure title titleHuman insulin receptor bound with A62-dimer, Pseudo-gamma conformation
Keywords keywordsSignaling, aptamer, agonist, complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.67
Radius of gyration Rg (electron density) rg_electron48.36
Forward intensity I(0) i0531240000.00
Molecular weight molecular_weight184090.0 kDa
Excluded volume excluded_volume227540 ų
Envelope volume envelope_volume357170 ų
Hydration-shell volume shell_volume63483 ų
Envelope diameter envelope_diameter157.5
Shell Rg shell_rg51.98
Envelope Rg envelope_rg45.74
Shape Rg shape_rg48.35
Total Rg total_rg48.54
Total atoms total_atoms12906
Residues n_residues1534
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 dmax153.3
Rg (real space) rg_real48.58
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real5.3120e+08
I(0) uncertainty (real space) i0_real_error9.7080e+06
Rg (reciprocal space) rg_reciprocal48.67
I(0) (reciprocal space) i0_reciprocal531300000.0000
Solution quality estimate total_estimate0.8812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.3
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.586
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18720000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.557

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)