8x5k

The Crystal Structure of SYK from Biortus.

Method: X-RAY DIFFRACTION Dmax: 64.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 356–635 Not recorded 3YT 2-{[(1R,2S)-2-aminocyclohexyl]amino}-4-{[3-(2H-1,2,3-triazol-2-yl)phenyl]amino}pyrimidine-5-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M Li2SO4, 0.1M Bis-Tris pH6.5, 25% PEG 3350 Resolution 1.80 Å R-free 0.244

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 1–280; 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 8x5k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x5k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x5k
Deposition date deposition_date2023-11-17
最后修订 last_revision2023-12-27
Structure title titleThe Crystal Structure of SYK from Biortus.
Keywords keywordsKinase Adaptive immunity, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.87
Radius of gyration Rg (electron density) rg_electron18.81
Forward intensity I(0) i016522200.00
Molecular weight molecular_weight31017.0 kDa
Excluded volume excluded_volume38958 ų
Envelope volume envelope_volume45396 ų
Hydration-shell volume shell_volume19955 ų
Envelope diameter envelope_diameter66.5
Shell Rg shell_rg25.38
Envelope Rg envelope_rg19.20
Shape Rg shape_rg18.79
Total Rg total_rg19.81
Total atoms total_atoms2177
Residues n_residues264
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 dmax64.0
Rg (real space) rg_real19.78
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.6520e+07
I(0) uncertainty (real space) i0_real_error2.3040e+05
Rg (reciprocal space) rg_reciprocal19.79
I(0) (reciprocal space) i0_reciprocal16520000.0000
Solution quality estimate total_estimate0.8143
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6254000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)