7v3p

Cryo-EM structure of the IGF1R/insulin complex

Method: ELECTRON MICROSCOPY Dmax: 170.0 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 1–931 Chain B; UniProt 1–931 Not recorded Insulin A chain × 1 (P01308) Insulin B chain × 1 (P01308) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 1–931; UniProt 1–931 Author chain B; PDBConstruct 1–931; UniProt 1–931

Insulin A chain

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 90–110 Chain F; UniProt 25–54 Not recorded Insulin-like growth factor 1 receptor × 2 (P08069) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 2, 3
Chains and sequence ranges Author chain E; PDBConstruct 1–21; UniProt 90–110 Author chain F; 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 7v3p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v3p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v3p
Deposition date deposition_date2021-08-11
Structure title titleCryo-EM structure of the IGF1R/insulin complex
Keywords keywordsThe type 1 insulin-like growth factor receptor (IGF1R), MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.58
Radius of gyration Rg (electron density) rg_electron49.54
Forward intensity I(0) i0558186000.00
Molecular weight molecular_weight192480.0 kDa
Excluded volume excluded_volume239670 ų
Envelope volume envelope_volume379070 ų
Hydration-shell volume shell_volume66237 ų
Envelope diameter envelope_diameter181.2
Shell Rg shell_rg51.70
Envelope Rg envelope_rg47.57
Shape Rg shape_rg49.54
Total Rg total_rg49.64
Total atoms total_atoms26387
Residues n_residues1674
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 dmax170.0
Rg (real space) rg_real49.80
Rg uncertainty (real space) rg_real_error2.04
I(0) (real space) i0_real5.5820e+08
I(0) uncertainty (real space) i0_real_error1.0770e+07
Rg (reciprocal space) rg_reciprocal49.59
I(0) (reciprocal space) i0_reciprocal558000000.0000
Solution quality estimate total_estimate0.8755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.1
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37690000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.831

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7v3pB01
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology20 — 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
Homologous superfamily homologous superfamily20 — Receptor L-domain
Domain ID domain_id7v3pB02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology220 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Homologous superfamily homologous superfamily10 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2

8. Citations (1)

9. Files and Curves (10)