10dj

Fyn Kinase Domain-Saracatinib Complex Structure

Method: X-RAY DIFFRACTION Dmax: 105.3 Å Quality: GOOD

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

Tyrosine-protein kinase Fyn

Homo sapiens

UniProt P06241

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 263–537 Not recorded H8H N-(5-CHLORO-1,3-BENZODIOXOL-4-YL)-7-[2-(4-METHYLPIPERAZIN-1-YL)ETHOXY]-5-(TETRAHYDRO-2H-PYRAN-4-YLOXY)QUINAZOLIN-4-AMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;4.0 M ammonium acetate, 0.1 M sodium acetate trihydrate, pH 4.6 Resolution 2.22 Å R-free 0.268
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 263–537 Not recorded H8H N-(5-CHLORO-1,3-BENZODIOXOL-4-YL)-7-[2-(4-METHYLPIPERAZIN-1-YL)ETHOXY]-5-(TETRAHYDRO-2H-PYRAN-4-YLOXY)QUINAZOLIN-4-AMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;4.0 M ammonium acetate, 0.1 M sodium acetate trihydrate, pH 4.6 Resolution 2.22 Å R-free 0.268

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.

50 other PDB entries and 67 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FYN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–275; UniProt 263–537 Author chain B; PDBConstruct 1–275; UniProt 263–537

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 10dj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id10dj
Deposition date deposition_date2026-01-13
Structure title titleFyn Kinase Domain-Saracatinib Complex Structure
Keywords keywordsTyrosine-protein kinase Fyn, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.09
Radius of gyration Rg (electron density) rg_electron29.79
Forward intensity I(0) i059690500.00
Molecular weight molecular_weight62615.0 kDa
Excluded volume excluded_volume79104 ų
Envelope volume envelope_volume99015 ų
Hydration-shell volume shell_volume28710 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg35.71
Envelope Rg envelope_rg29.87
Shape Rg shape_rg29.78
Total Rg total_rg30.39
Total atoms total_atoms8756
Residues n_residues546
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 dmax105.3
Rg (real space) rg_real30.24
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real5.9690e+07
I(0) uncertainty (real space) i0_real_error9.4310e+05
Rg (reciprocal space) rg_reciprocal30.18
I(0) (reciprocal space) i0_reciprocal59690000.0000
Solution quality estimate total_estimate0.8464
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.408
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18590000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.778; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)