9pvo

Novel site 1 interaction of the IR/Ins-AC-S2 complex

Method: ELECTRON MICROSCOPY Dmax: 118.5 Å Quality: GOOD

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

Isoform Long of 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 28–956 Chain B; UniProt 28–956 Not recorded Insulin chain A × 1 Insulin chain B × 1 (P01308) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.89 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 1–929; UniProt 28–956 Author chain B; PDBConstruct 1–929; UniProt 28–956

Insulin chain B

OrganismNot specified

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 R; UniProt 25–53 Not recorded Isoform Long of Insulin receptor × 2 (P06213) Insulin chain A × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.89 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
Chains and sequence ranges Author chain R; PDBConstruct 1–29; UniProt 25–53

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 9pvo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pvo
Deposition date deposition_date2025-08-03
Structure title titleNovel site 1 interaction of the IR/Ins-AC-S2 complex
Keywords keywordsAntagonism, receptor tyrosine kinase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.29
Radius of gyration Rg (electron density) rg_electron36.53
Forward intensity I(0) i0132400000.00
Molecular weight molecular_weight91729.0 kDa
Excluded volume excluded_volume114430 ų
Envelope volume envelope_volume163460 ų
Hydration-shell volume shell_volume37828 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg42.55
Envelope Rg envelope_rg35.03
Shape Rg shape_rg36.51
Total Rg total_rg37.00
Total atoms total_atoms12697
Residues n_residues801
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 dmax118.5
Rg (real space) rg_real37.18
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.3240e+08
I(0) uncertainty (real space) i0_real_error2.1530e+06
Rg (reciprocal space) rg_reciprocal37.25
I(0) (reciprocal space) i0_reciprocal132400000.0000
Solution quality estimate total_estimate0.8319
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.770
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha9816000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)