8u4e

Cryo-EM structure of long form insulin receptor (IR-B) with three IGF2 bound, asymmetric conformation.

Method: ELECTRON MICROSCOPY Dmax: 172.7 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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1382 Chain B; UniProt 1–1382 Not recorded Insulin-like growth factor II × 3 (P01344) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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
Chains and sequence ranges Author chain A; PDBConstruct 1–1382; UniProt 1–1382 Author chain B; PDBConstruct 1–1382; UniProt 1–1382

Insulin-like growth factor II

Homo sapiens

UniProt P01344

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–180 Chain D; UniProt 1–180 Chain E; UniProt 1–180 Not recorded Insulin receptor × 2 (P06213) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGF2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–180; UniProt 1–180 Author chain D; PDBConstruct 1–180; UniProt 1–180 Author chain E; PDBConstruct 1–180; UniProt 1–180

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 8u4e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u4e
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8u4e
Deposition date deposition_date2023-09-10
Structure title titleCryo-EM structure of long form insulin receptor (IR-B) with three IGF2 bound, asymmetric conformation.
Keywords keywordsInsulin receptor, IGF2, RTK, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.09
Radius of gyration Rg (electron density) rg_electron51.73
Forward intensity I(0) i0585138000.00
Molecular weight molecular_weight198590.0 kDa
Excluded volume excluded_volume247720 ų
Envelope volume envelope_volume392310 ų
Hydration-shell volume shell_volume66811 ų
Envelope diameter envelope_diameter174.8
Shell Rg shell_rg52.50
Envelope Rg envelope_rg48.92
Shape Rg shape_rg51.71
Total Rg total_rg51.84
Total atoms total_atoms13948
Residues n_residues1729
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 dmax172.7
Rg (real space) rg_real52.09
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real5.8510e+08
I(0) uncertainty (real space) i0_real_error1.0490e+07
Rg (reciprocal space) rg_reciprocal52.07
I(0) (reciprocal space) i0_reciprocal585100000.0000
Solution quality estimate total_estimate0.8924
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.3
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.572
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23780000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)