6ceb

Insulin Receptor ectodomain in complex with two insulin molecules - C1 symmetry

Method: ELECTRON MICROSCOPY Dmax: 151.0 Å Quality: GOOD

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

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 Other combination Heteromer Protein × 8 其他Polymer 10 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 28–944 Chain B; UniProt 28–944 Chain M; UniProt 718–747 Chain P; UniProt 718–747 Fragment:Ectodomain residues 28-944 Fragment:residues 718-747 Insulin A chain × 2 (P01308) Insulin B chain × 2 (P01318) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Hepes Saline (HBS) cryo-EM vitrification conditions:Cryogen ETHANE;Grids made with SpotItOn Resolution 4.70 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.

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 P06213-2
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–917; UniProt 28–944 Author chain B; PDBConstruct 1–917; UniProt 28–944 Author chain M; PDBConstruct 1–30; UniProt 718–747 Author chain P; PDBConstruct 1–30; UniProt 718–747

Insulin A chain

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 Other combination Heteromer Protein × 8 其他Polymer 10 PDB declaration: octameric(8) Consistent with protein copy count Chain K; UniProt 90–110 Chain N; UniProt 90–110 Not recorded Insulin receptor × 2 (P06213) Insulin receptor × 2 (P06213) Insulin B chain × 2 (P01318) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Hepes Saline (HBS) cryo-EM vitrification conditions:Cryogen ETHANE;Grids made with SpotItOn Resolution 4.70 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.

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 K; PDBConstruct 1–21; UniProt 90–110 Author chain N; PDBConstruct 1–21; UniProt 90–110

Insulin B chain

OrganismNot specified

UniProt P01318

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 × 8 其他Polymer 10 PDB declaration: octameric(8) Consistent with protein copy count Chain L; UniProt 25–54 Chain O; UniProt 25–54 Not recorded Insulin receptor × 2 (P06213) Insulin receptor × 2 (P06213) Insulin A chain × 2 (P01308) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 4 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Hepes Saline (HBS) cryo-EM vitrification conditions:Cryogen ETHANE;Grids made with SpotItOn Resolution 4.70 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.

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

View Construct and Data Evidence
UniProt name INS_SHEEP
Isoform
PDB entities 4
Chains and sequence ranges Author chain L; PDBConstruct 1–30; UniProt 25–54 Author chain O; 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 6ceb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ceb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ceb
Deposition date deposition_date2018-02-11
Structure title titleInsulin Receptor ectodomain in complex with two insulin molecules - C1 symmetry
Keywords keywordssignaling, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.71
Radius of gyration Rg (electron density) rg_electron45.33
Forward intensity I(0) i0422930000.00
Molecular weight molecular_weight167160.0 kDa
Excluded volume excluded_volume208470 ų
Envelope volume envelope_volume319600 ų
Hydration-shell volume shell_volume60526 ų
Envelope diameter envelope_diameter151.5
Shell Rg shell_rg47.88
Envelope Rg envelope_rg44.93
Shape Rg shape_rg45.26
Total Rg total_rg45.70
Total atoms total_atoms11722
Residues n_residues1406
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 dmax151.0
Rg (real space) rg_real45.78
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real4.2290e+08
I(0) uncertainty (real space) i0_real_error8.3260e+06
Rg (reciprocal space) rg_reciprocal45.71
I(0) (reciprocal space) i0_reciprocal422900000.0000
Solution quality estimate total_estimate0.8249
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.5
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.642
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36930000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)