10oo

FGFR2 mutant D650V with compound 4 (AZD3463)

Method: X-RAY DIFFRACTION Dmax: 84.3 Å Quality: EXCELLENT

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

Fibroblast growth factor receptor 2

Homo sapiens

UniProt P21802

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 A; UniProt 458–768 Mutation:D650V A1C65 (4P)-N-[4-(4-aminopiperidin-1-yl)-2-methoxyphenyl]-5-chloro-4-(1H-indol-3-yl)pyrimidin-2-amine × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;30% PEG 4,000, 200 mM Lithium Sulfate, 100 mM TRIS pH 8.5 Resolution 1.85 Å R-free 0.256
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 458–768 Mutation:D650V A1C65 (4P)-N-[4-(4-aminopiperidin-1-yl)-2-methoxyphenyl]-5-chloro-4-(1H-indol-3-yl)pyrimidin-2-amine × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;293 K;30% PEG 4,000, 200 mM Lithium Sulfate, 100 mM TRIS pH 8.5 Resolution 1.85 Å R-free 0.256

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.

60 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGFR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–324; UniProt 458–768 Author chain B; PDBConstruct 14–324; UniProt 458–768

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 10oo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10oo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10oo
Deposition date deposition_date2026-01-29
最后修订 last_revision2026-04-15
Structure title titleFGFR2 mutant D650V with compound 4 (AZD3463)
Keywords keywordsFGFR2, FGFR, Fibroblast growth factor receptor, Tyrosine Kinase, Resistance Mutations, AZD3463, compound 4, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.51
Radius of gyration Rg (electron density) rg_electron25.81
Forward intensity I(0) i0134410000.00
Molecular weight molecular_weight60928.0 kDa
Excluded volume excluded_volume58788 ų
Envelope volume envelope_volume100320 ų
Hydration-shell volume shell_volume31942 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg33.45
Envelope Rg envelope_rg25.72
Shape Rg shape_rg25.80
Total Rg total_rg26.41
Total atoms total_atoms4582
Residues n_residues561
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 dmax84.3
Rg (real space) rg_real26.42
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.3440e+08
I(0) uncertainty (real space) i0_real_error1.6960e+06
Rg (reciprocal space) rg_reciprocal26.45
I(0) (reciprocal space) i0_reciprocal134400000.0000
Solution quality estimate total_estimate0.9059
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35490000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)