8pyi

Human IGF1R with inhibitor 6

Method: X-RAY DIFFRACTION Dmax: 127.8 Å Quality: GOOD

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

Insulin-like growth factor 1 receptor beta chain

Homo sapiens

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain AAA; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain BBB; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain CCC; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain DDD; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain EEE; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain FFF; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain GGG; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain HHH; UniProt 974–1286 Not recorded IER 3-[8-azanyl-1-(4-ethoxy-8-fluoranyl-2-phenyl-quinolin-7-yl)imidazo[1,5-a]pyrazin-3-yl]-1-methyl-cyclobutan-1-ol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.1 M Bis-Tris, 0.3 M MgCl2, 20% PEG 3350 Resolution 3.06 Å R-free 0.235

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 85 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 AAA; PDBConstruct 2–314; UniProt 974–1286 Author chain BBB; PDBConstruct 2–314; UniProt 974–1286 Author chain CCC; PDBConstruct 2–314; UniProt 974–1286 Author chain DDD; PDBConstruct 2–314; UniProt 974–1286 Author chain EEE; PDBConstruct 2–314; UniProt 974–1286 Author chain FFF; PDBConstruct 2–314; UniProt 974–1286 Author chain GGG; PDBConstruct 2–314; UniProt 974–1286 Author chain HHH; PDBConstruct 2–314; UniProt 974–1286

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 8pyi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pyi
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8pyi
Deposition date deposition_date2023-07-25
最后修订 last_revision2023-09-20
Structure title titleHuman IGF1R with inhibitor 6
Keywords keywordsTyrosine, Kinase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.25
Radius of gyration Rg (electron density) rg_electron41.53
Forward intensity I(0) i01029080000.00
Molecular weight molecular_weight266500.0 kDa
Excluded volume excluded_volume333630 ų
Envelope volume envelope_volume443180 ų
Hydration-shell volume shell_volume84313 ų
Envelope diameter envelope_diameter132.9
Shell Rg shell_rg50.52
Envelope Rg envelope_rg40.74
Shape Rg shape_rg41.52
Total Rg total_rg42.00
Total atoms total_atoms18686
Residues n_residues2289
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 dmax127.8
Rg (real space) rg_real41.96
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.0290e+09
I(0) uncertainty (real space) i0_real_error1.7390e+07
Rg (reciprocal space) rg_reciprocal42.24
I(0) (reciprocal space) i0_reciprocal1029000000.0000
Solution quality estimate total_estimate0.8934
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.2
Skewness Skewness skewness0.047
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98900000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)