8u1f

FGFR2 Kinase Domain Bound to Irreversible Inhibitor Cmpd 10

Method: X-RAY DIFFRACTION Dmax: 86.5 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 458–768 Chain B; UniProt 458–768 Not recorded GOL GLYCEROL × 1 UIM N-[4-(4-amino-7-methyl-5-{4-[(4-methylpyrimidin-2-yl)oxy]phenyl}-7H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]-2-methylpropanamide × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291.15 K;0.1 M Tris pH 8, 18% PEG K Resolution 3.33 Å R-free 0.295

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 123 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 6–316; UniProt 458–768 Author chain B; PDBConstruct 6–316; 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 8u1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u1f
Deposition date deposition_date2023-08-31
Structure title titleFGFR2 Kinase Domain Bound to Irreversible Inhibitor Cmpd 10
Keywords keywordsInhibitor Kinase, ONCOPROTEIN, Transferase-Inhibitor complex; Transferase/Inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.34
Radius of gyration Rg (electron density) rg_electron27.47
Forward intensity I(0) i063188000.00
Molecular weight molecular_weight63092.0 kDa
Excluded volume excluded_volume79395 ų
Envelope volume envelope_volume101840 ų
Hydration-shell volume shell_volume30673 ų
Envelope diameter envelope_diameter91.8
Shell Rg shell_rg35.17
Envelope Rg envelope_rg27.19
Shape Rg shape_rg27.45
Total Rg total_rg28.35
Total atoms total_atoms8839
Residues n_residues544
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 dmax86.5
Rg (real space) rg_real28.26
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real6.3190e+07
I(0) uncertainty (real space) i0_real_error8.5410e+05
Rg (reciprocal space) rg_reciprocal28.29
I(0) (reciprocal space) i0_reciprocal63190000.0000
Solution quality estimate total_estimate0.9102
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary85.0
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.602
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24470000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)