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9hkt

Drosophila melanogaster insulin receptor ectodomain in complex with one DILP2 molecule

Method: ELECTRON MICROSCOPY Dmax: 176.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 264–1310 Chain B； UniProt 264–1310 Not recorded Probable insulin-like peptide 2 × 1 （Q9VT51） Probable insulin-like peptide 2 × 1 （Q9VT51） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 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 3.70 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.

Other PDB Difference from Current Entry 9HKT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8CLS Drosophila melanogaster insulin receptor ectodomain in complex with DILP5 Deposited 2023-02-17 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 264–1310（1047 aa）
Chain B 264–1310（1047 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
9EF1 Cryo-EM structure of Drosophila melanogaster insulin receptor (dmIR) bound with one DILP1, asymmetric conformation Deposited 2024-11-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–2144（2144 aa）
Chain B 1–2144（2144 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
9EF4 Cryo-EM structure of Drosophila melanogaster insulin receptor (dmIR) bound with two DILP1, symmetric conformation Deposited 2024-11-19 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–2144（2144 aa）
Chain B 1–2144（2144 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
9EF5 Cryo-EM structure of Drosophila melanogaster insulin receptor (dmIR) bound with one DILP2, asymmetric conformation Deposited 2024-11-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–2144（2144 aa）
Chain B 1–2144（2144 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
9EF9 Cryo-EM structure of Drosophila melanogaster insulin receptor (dmIR) bound with three DILP5, asymmetric conformation Deposited 2024-11-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–2144（2144 aa）
Chain B 1–2144（2144 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9HNI Drosophila melanogaster insulin receptor ectodomain in complex with two DILP2 molecules Deposited 2024-12-10 Different oligomeric state Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 264–1310（1047 aa）
Chain B 264–1310（1047 aa）
Not recorded 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

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 1
Chains and sequence ranges Author chain A； PDBConstruct 2–1048； UniProt 264–1310 Author chain B； PDBConstruct 2–1048； UniProt 264–1310

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 × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count 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 × 4 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 3.70 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.

Other PDB Difference from Current Entry 9HKT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9EF5 Cryo-EM structure of Drosophila melanogaster insulin receptor (dmIR) bound with one DILP2, asymmetric conformation Deposited 2024-11-19 Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 27–50（24 aa）
Chain D 112–137（26 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
9HNI Drosophila melanogaster insulin receptor ectodomain in complex with two DILP2 molecules Deposited 2024-12-10 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 112–137（26 aa）
Chain F 27–50（24 aa）
Chain G 112–137（26 aa）
Chain H 27–50（24 aa）
Not recorded 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

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 2, 3
Chains and sequence ranges Author chain G； PDBConstruct 1–26； UniProt 112–137 Author chain H； PDBConstruct 1–24； UniProt 27–50

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 9hkt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hkt
Deposition date deposition_date2024-12-04
Structure title titleDrosophila melanogaster insulin receptor ectodomain in complex with one DILP2 molecule
Keywords keywordsReceptor, Dilp2, Drosophila, complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier51.99 Å
Radius of gyration Rg (electron density) rg_electron51.83 Å
Forward intensity I(0) i0623096000.00
Molecular weight molecular_weight203090.0 kDa
Excluded volume excluded_volume252750 ų
Envelope volume envelope_volume413790 ų
Hydration-shell volume shell_volume69300 ų
Envelope diameter envelope_diameter172.9 Å
Shell Rg shell_rg53.40 Å
Envelope Rg envelope_rg49.57 Å
Shape Rg shape_rg51.80 Å
Total Rg total_rg51.99 Å
Total atoms total_atoms14220
Residues n_residues1748
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax176.2 Å
Rg (real space) rg_real51.99 Å
Rg uncertainty (real space) rg_real_error2.09 Å
I(0) (real space) i0_real6.2310e+08
I(0) uncertainty (real space) i0_real_error1.3300e+07
Rg (reciprocal space) rg_reciprocal51.97 Å
I(0) (reciprocal space) i0_reciprocal623100000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.6 Å
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.1500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26050000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.878
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)