8dtl

Cryo-EM structure of insulin receptor (IR) bound with S597 peptide

Method: ELECTRON MICROSCOPY Dmax: 172.5 Å Quality: GOOD

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

Insulin receptor

Mus musculus

UniProt P15208

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 28–1372 Chain B; UniProt 28–1372 Not recorded Insulin mimetic peptide S597 × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSR_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–1345; UniProt 28–1372 Author chain B; PDBConstruct 1–1345; UniProt 28–1372

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 8dtl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dtl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dtl
Deposition date deposition_date2022-07-25
Structure title titleCryo-EM structure of insulin receptor (IR) bound with S597 peptide
Keywords keywordsInsulin receptor, S597, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.20
Radius of gyration Rg (electron density) rg_electron54.88
Forward intensity I(0) i0465355000.00
Molecular weight molecular_weight177980.0 kDa
Excluded volume excluded_volume222420 ų
Envelope volume envelope_volume379770 ų
Hydration-shell volume shell_volume62522 ų
Envelope diameter envelope_diameter175.2
Shell Rg shell_rg52.79
Envelope Rg envelope_rg51.46
Shape Rg shape_rg54.83
Total Rg total_rg54.98
Total atoms total_atoms12512
Residues n_residues1544
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 dmax172.5
Rg (real space) rg_real55.14
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real4.6540e+08
I(0) uncertainty (real space) i0_real_error8.7570e+06
Rg (reciprocal space) rg_reciprocal55.22
I(0) (reciprocal space) i0_reciprocal465400000.0000
Solution quality estimate total_estimate0.8485
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.1
Skewness Skewness skewness0.109
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.145

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)