8wyw

Crystal structure of spleen tyrosine kinase (SYK) in complex with SKI-O-592 (free form of SKI-O-703, cevidoplenib)

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: GOOD

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

Tyrosine-protein kinase SYK

Homo sapiens

UniProt P43405

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 356–635 Chain B; UniProt 356–635 Fragment:UNP residues 356-635 XFB SKI-O-592 × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100mM Sodium-HEPES 7.0, 15%(v/v)PEG 4000 Resolution 1.90 Å R-free 0.242

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.

92 other PDB entries and 134 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KSYK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–283; UniProt 356–635 Author chain B; PDBConstruct 4–283; UniProt 356–635

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 8wyw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wyw
Deposition date deposition_date2023-10-31
最后修订 last_revision2024-11-06
Structure title titleCrystal structure of spleen tyrosine kinase (SYK) in complex with SKI-O-592 (free form of SKI-O-703, cevidoplenib)
Keywords keywordstransferase, signal pathway, anticancer; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.69
Radius of gyration Rg (electron density) rg_electron29.48
Forward intensity I(0) i060305500.00
Molecular weight molecular_weight62001.0 kDa
Excluded volume excluded_volume77986 ų
Envelope volume envelope_volume95890 ų
Hydration-shell volume shell_volume28719 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg34.54
Envelope Rg envelope_rg29.77
Shape Rg shape_rg29.47
Total Rg total_rg30.01
Total atoms total_atoms4352
Residues n_residues527
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 dmax104.3
Rg (real space) rg_real29.95
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real6.0310e+07
I(0) uncertainty (real space) i0_real_error9.4470e+05
Rg (reciprocal space) rg_reciprocal29.84
I(0) (reciprocal space) i0_reciprocal60300000.0000
Solution quality estimate total_estimate0.8189
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.316
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16500000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.669; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.711; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)