8cls

Drosophila melanogaster insulin receptor ectodomain in complex with DILP5

Method: ELECTRON MICROSCOPY Dmax: 174.5 Å Quality: GOOD

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 264–1310 Chain B; UniProt 264–1310 Not recorded Probable insulin-like peptide 5 A chain × 3 (Q7KUD5) Probable insulin-like peptide 5 × 3 (Q7KUD5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 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 5 A chain

OrganismNot specified

UniProt Q7KUD5

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 84–108 Chain D; UniProt 24–51 Chain E; UniProt 84–108 Chain F; UniProt 24–51 Chain G; UniProt 84–108 Chain H; UniProt 24–51 Not recorded Insulin-like receptor × 2 (P09208) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INSL5_DROME
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain C; PDBConstruct 1–25; UniProt 84–108 Author chain E; PDBConstruct 1–25; UniProt 84–108 Author chain G; PDBConstruct 1–25; UniProt 84–108 Author chain D; PDBConstruct 1–28; UniProt 24–51 Author chain F; PDBConstruct 1–28; UniProt 24–51 Author chain H; PDBConstruct 1–28; UniProt 24–51

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 8cls

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8cls
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8cls
Deposition date deposition_date2023-02-17
Structure title titleDrosophila melanogaster insulin receptor ectodomain in complex with DILP5
Keywords keywordsDILP5 hormone, Drosophila insulin-like signalling receptor, disulfide linked ectodomain, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.47
Radius of gyration Rg (electron density) rg_electron51.49
Forward intensity I(0) i0635363000.00
Molecular weight molecular_weight204170.0 kDa
Excluded volume excluded_volume253440 ų
Envelope volume envelope_volume389300 ų
Hydration-shell volume shell_volume65974 ų
Envelope diameter envelope_diameter186.0
Shell Rg shell_rg52.61
Envelope Rg envelope_rg49.76
Shape Rg shape_rg51.48
Total Rg total_rg51.58
Total atoms total_atoms28081
Residues n_residues1840
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 dmax174.5
Rg (real space) rg_real51.51
Rg uncertainty (real space) rg_real_error2.01
I(0) (real space) i0_real6.3540e+08
I(0) uncertainty (real space) i0_real_error1.3580e+07
Rg (reciprocal space) rg_reciprocal51.41
I(0) (reciprocal space) i0_reciprocal635300000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.9
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28870000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)