6vwj

Leg region of the closed conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II

Method: ELECTRON MICROSCOPY Dmax: 113.4 Å Quality: GOOD

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

Leucine-zippered human type 1 insulin-like growth factor receptor ectodomain

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P03069

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 249–281 Chain B; UniProt 249–281 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.21 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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 906–938; UniProt 249–281 Author chain B; PDBConstruct 906–938; UniProt 249–281

Leucine-zippered human type 1 insulin-like growth factor receptor ectodomain

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P08069

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 31–935 Chain B; UniProt 31–935 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.21 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.

44 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGF1R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–905; UniProt 31–935 Author chain B; PDBConstruct 1–905; UniProt 31–935

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 6vwj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6vwj
Deposition date deposition_date2020-02-19
Structure title titleLeg region of the closed conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II
Keywords keywordsType 1 insulin-like growth factor receptor, Insulin-like growth factor II, ectodomain receptor, tyrosine kinase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.45
Radius of gyration Rg (electron density) rg_electron32.78
Forward intensity I(0) i0120646000.00
Molecular weight molecular_weight85456.0 kDa
Excluded volume excluded_volume106220 ų
Envelope volume envelope_volume148950 ų
Hydration-shell volume shell_volume38789 ų
Envelope diameter envelope_diameter124.2
Shell Rg shell_rg38.53
Envelope Rg envelope_rg32.42
Shape Rg shape_rg32.80
Total Rg total_rg33.19
Total atoms total_atoms11799
Residues n_residues747
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 dmax113.4
Rg (real space) rg_real33.42
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.2060e+08
I(0) uncertainty (real space) i0_real_error2.1520e+06
Rg (reciprocal space) rg_reciprocal33.44
I(0) (reciprocal space) i0_reciprocal120600000.0000
Solution quality estimate total_estimate0.8846
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.4
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.280
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11860000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)