6sof

human insulin receptor ectodomain bound by 4 insulin

Method: ELECTRON MICROSCOPY Dmax: 167.8 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 28–746 Chain B; UniProt 783–944 Chain C; UniProt 28–746 Chain D; UniProt 783–944 Not recorded Insulin × 4 (P01308) Insulin × 4 (P01308) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–719; UniProt 28–746 Author chain C; PDBConstruct 1–719; UniProt 28–746 Author chain B; PDBConstruct 1–162; UniProt 783–944 Author chain D; PDBConstruct 1–162; UniProt 783–944

Insulin

Homo sapiens

UniProt P01308

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 90–110 Chain F; UniProt 25–54 Chain G; UniProt 90–110 Chain H; UniProt 25–54 Chain I; UniProt 90–110 Chain J; UniProt 25–54 Chain K; UniProt 90–110 Chain L; UniProt 25–54 Not recorded Insulin receptor × 2 (P06213) Insulin receptor × 2 (P06213) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.30 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.

369 other PDB entries and 583 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain E; PDBConstruct 1–21; UniProt 90–110 Author chain G; PDBConstruct 1–21; UniProt 90–110 Author chain I; PDBConstruct 1–21; UniProt 90–110 Author chain K; PDBConstruct 1–21; UniProt 90–110 Author chain F; PDBConstruct 1–30; UniProt 25–54 Author chain H; PDBConstruct 1–30; UniProt 25–54 Author chain J; PDBConstruct 1–30; UniProt 25–54 Author chain L; PDBConstruct 1–30; UniProt 25–54

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 6sof

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sof
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sof
Deposition date deposition_date2019-08-29
Structure title titlehuman insulin receptor ectodomain bound by 4 insulin
Keywords keywordscell surface receptor, insulin, tyrosine kinase receptor, glucose homeostasis, hormone, diabetes, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.53
Radius of gyration Rg (electron density) rg_electron50.45
Forward intensity I(0) i0765657000.00
Molecular weight molecular_weight224610.0 kDa
Excluded volume excluded_volume279080 ų
Envelope volume envelope_volume429010 ų
Hydration-shell volume shell_volume74531 ų
Envelope diameter envelope_diameter168.9
Shell Rg shell_rg51.01
Envelope Rg envelope_rg48.98
Shape Rg shape_rg50.45
Total Rg total_rg50.50
Total atoms total_atoms30333
Residues n_residues1966
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 dmax167.8
Rg (real space) rg_real50.55
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real7.6570e+08
I(0) uncertainty (real space) i0_real_error1.3790e+07
Rg (reciprocal space) rg_reciprocal50.51
I(0) (reciprocal space) i0_reciprocal765600000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.1
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57760000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.759

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)