9nco

IN-ML-15 bound to IGF1Rzip

Method: ELECTRON MICROSCOPY Dmax: 160.9 Å Quality: GOOD

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

Insulin-like growth factor 1 receptor

Homo sapiens

UniProt P08069

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 31–926 Chain B; UniProt 31–926 Not recorded IN-ML-15 beta × 1 IN-ML-15 alpha × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

44 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGF1R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–896; UniProt 31–926 Author chain B; PDBConstruct 1–896; UniProt 31–926

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 9nco

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9nco
Deposition date deposition_date2025-02-16
Structure title titleIN-ML-15 bound to IGF1Rzip
Keywords keywordsIGF receptor, insulin-like growth factor, insulin, IGF, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.07
Radius of gyration Rg (electron density) rg_electron46.80
Forward intensity I(0) i0568287000.00
Molecular weight molecular_weight193690.0 kDa
Excluded volume excluded_volume241000 ų
Envelope volume envelope_volume359860 ų
Hydration-shell volume shell_volume65260 ų
Envelope diameter envelope_diameter166.4
Shell Rg shell_rg50.75
Envelope Rg envelope_rg45.13
Shape Rg shape_rg46.79
Total Rg total_rg47.03
Total atoms total_atoms13604
Residues n_residues1693
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 dmax160.9
Rg (real space) rg_real47.18
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real5.6830e+08
I(0) uncertainty (real space) i0_real_error1.1680e+07
Rg (reciprocal space) rg_reciprocal47.07
I(0) (reciprocal space) i0_reciprocal568200000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37530000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)