8e1x

FGFR2 kinase domain in complex with a Pyrazolo[1,5-a]pyrimidine analog (Compound 29)

Method: X-RAY DIFFRACTION Dmax: 87.0 Å Quality: GOOD

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 459–768 Chain B; UniProt 459–768 Non-standard monomer:Yes (specific site not provided by mmCIF) U9P (5M)-N-methyl-5-{(6M,8S)-5-{[(3S)-oxolan-3-yl]amino}-6-[1-(propan-2-yl)-1H-pyrazol-3-yl]pyrazolo[1,5-a]pyrimidin-3-yl}pyridine-3-carboxamide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.2;293 K;0.1 M Sodium citrate pH 5.2; 28% w/w PEG 4,000; 0.2 M Ammonium acetate Resolution 2.68 Å R-free 0.272

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 21–330; UniProt 459–768 Author chain B; PDBConstruct 21–330; UniProt 459–768

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 8e1x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e1x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e1x
Deposition date deposition_date2022-08-11
Structure title titleFGFR2 kinase domain in complex with a Pyrazolo[1,5-a]pyrimidine analog (Compound 29)
Keywords keywordsFGFR, inhibitor, kinase, gatekeeper, hyperphosphatemia, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.98
Radius of gyration Rg (electron density) rg_electron26.02
Forward intensity I(0) i069483900.00
Molecular weight molecular_weight64531.0 kDa
Excluded volume excluded_volume80587 ų
Envelope volume envelope_volume102480 ų
Hydration-shell volume shell_volume32406 ų
Envelope diameter envelope_diameter90.7
Shell Rg shell_rg33.70
Envelope Rg envelope_rg26.11
Shape Rg shape_rg26.03
Total Rg total_rg26.86
Total atoms total_atoms4521
Residues n_residues579
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 dmax87.0
Rg (real space) rg_real26.90
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real6.9480e+07
I(0) uncertainty (real space) i0_real_error9.8190e+05
Rg (reciprocal space) rg_reciprocal26.92
I(0) (reciprocal space) i0_reciprocal69490000.0000
Solution quality estimate total_estimate0.8201
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary31.0
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36490000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)