7q63

The tandem SH2 domains of SYK

Method: X-RAY DIFFRACTION Dmax: 114.4 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain AAA; UniProt 6–269 Not recorded PEG DI(HYDROXYETHYL)ETHER × 1 SCN THIOCYANATE ION × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;200 mM, potassium thiocyanate, 12.5% glycerol, 23% PEG3350 Resolution 1.90 Å R-free 0.264
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain BBB; UniProt 6–269 Not recorded SCN THIOCYANATE ION × 4 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;200 mM, potassium thiocyanate, 12.5% glycerol, 23% PEG3350 Resolution 1.90 Å R-free 0.264
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain CCC; UniProt 6–269 Not recorded SCN THIOCYANATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;200 mM, potassium thiocyanate, 12.5% glycerol, 23% PEG3350 Resolution 1.90 Å R-free 0.264

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 132 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 AAA; PDBConstruct 2–265; UniProt 6–269 Author chain BBB; PDBConstruct 2–265; UniProt 6–269 Author chain CCC; PDBConstruct 2–265; UniProt 6–269

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 7q63

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q63
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q63
Deposition date deposition_date2021-11-05
Structure title titleThe tandem SH2 domains of SYK
Keywords keywordsSignalling, kinase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.94
Radius of gyration Rg (electron density) rg_electron35.31
Forward intensity I(0) i0114937000.00
Molecular weight molecular_weight84711.0 kDa
Excluded volume excluded_volume105730 ų
Envelope volume envelope_volume151820 ų
Hydration-shell volume shell_volume36488 ų
Envelope diameter envelope_diameter126.1
Shell Rg shell_rg40.92
Envelope Rg envelope_rg34.52
Shape Rg shape_rg35.32
Total Rg total_rg35.73
Total atoms total_atoms5967
Residues n_residues743
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 dmax114.4
Rg (real space) rg_real35.87
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real1.1490e+08
I(0) uncertainty (real space) i0_real_error1.8370e+06
Rg (reciprocal space) rg_reciprocal35.91
I(0) (reciprocal space) i0_reciprocal114900000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.564
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5877000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)