9hni

Drosophila melanogaster insulin receptor ectodomain in complex with two DILP2 molecules

Method: ELECTRON MICROSCOPY Dmax: 170.7 Å Quality: GOOD

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

Probable insulin-like peptide 2

OrganismNot specified

UniProt Q9VT51

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 112–137 Chain F; UniProt 27–50 Chain G; UniProt 112–137 Chain H; UniProt 27–50 Not recorded Insulin-like receptor × 2 (P09208) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM Hepes pH 7.5, 200mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.25 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSL2_DROME
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain E; PDBConstruct 1–26; UniProt 112–137 Author chain G; PDBConstruct 1–26; UniProt 112–137 Author chain F; PDBConstruct 1–24; UniProt 27–50 Author chain H; PDBConstruct 1–24; UniProt 27–50

Insulin-like receptor

Drosophila melanogaster

UniProt P09208

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 264–1310 Chain B; UniProt 264–1310 Not recorded Probable insulin-like peptide 2 × 2 (Q9VT51) Probable insulin-like peptide 2 × 2 (Q9VT51) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM Hepes pH 7.5, 200mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.25 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSR_DROME
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 2–1048; UniProt 264–1310 Author chain B; PDBConstruct 2–1048; UniProt 264–1310

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 9hni

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9hni
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9hni
Deposition date deposition_date2024-12-10
Structure title titleDrosophila melanogaster insulin receptor ectodomain in complex with two DILP2 molecules
Keywords keywordsReceptor, Dilp2, Drosophila, complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.95
Radius of gyration Rg (electron density) rg_electron50.79
Forward intensity I(0) i0634270000.00
Molecular weight molecular_weight204990.0 kDa
Excluded volume excluded_volume255190 ų
Envelope volume envelope_volume391170 ų
Hydration-shell volume shell_volume67529 ų
Envelope diameter envelope_diameter167.8
Shell Rg shell_rg52.41
Envelope Rg envelope_rg48.04
Shape Rg shape_rg50.78
Total Rg total_rg50.92
Total atoms total_atoms14354
Residues n_residues1774
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 dmax170.7
Rg (real space) rg_real50.92
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real6.3430e+08
I(0) uncertainty (real space) i0_real_error1.2410e+07
Rg (reciprocal space) rg_reciprocal50.95
I(0) (reciprocal space) i0_reciprocal634300000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.6
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.610
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22220000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)