7q5t

The tandem SH2 domains of SYK with a bound FCER1G diphospho-ITAM peptide

Method: X-RAY DIFFRACTION Dmax: 119.3 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain AAA; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain BBB; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) PO4 PHOSPHATE ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain CCC; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain DDD; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain EEE; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain FFF; UniProt 6–269 Not recorded High affinity immunoglobulin epsilon receptor subunit gamma × 1 (P30273) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255

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 129 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 Author chain DDD; PDBConstruct 2–265; UniProt 6–269 Author chain EEE; PDBConstruct 2–265; UniProt 6–269 Author chain FFF; PDBConstruct 2–265; UniProt 6–269

High affinity immunoglobulin epsilon receptor subunit gamma

OrganismNot specified

UniProt P30273

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain JJJ; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain KKK; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) PO4 PHOSPHATE ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain HHH; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) PO4 PHOSPHATE ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain III; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain GGG; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain LLL; UniProt 62–81 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein kinase SYK × 1 (P43405) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME Resolution 2.20 Å R-free 0.255

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCERG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain GGG; PDBConstruct 1–20; UniProt 62–81 Author chain HHH; PDBConstruct 1–20; UniProt 62–81 Author chain III; PDBConstruct 1–20; UniProt 62–81 Author chain JJJ; PDBConstruct 1–20; UniProt 62–81 Author chain KKK; PDBConstruct 1–20; UniProt 62–81 Author chain LLL; PDBConstruct 1–20; UniProt 62–81

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 7q5t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q5t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q5t
Deposition date deposition_date2021-11-04
Structure title titleThe tandem SH2 domains of SYK with a bound FCER1G diphospho-ITAM peptide
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_guinier38.91
Radius of gyration Rg (electron density) rg_electron38.27
Forward intensity I(0) i0547758000.00
Molecular weight molecular_weight186850.0 kDa
Excluded volume excluded_volume232580 ų
Envelope volume envelope_volume326590 ų
Hydration-shell volume shell_volume69287 ų
Envelope diameter envelope_diameter128.7
Shell Rg shell_rg45.92
Envelope Rg envelope_rg37.25
Shape Rg shape_rg38.27
Total Rg total_rg38.76
Total atoms total_atoms13154
Residues n_residues1618
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 dmax119.3
Rg (real space) rg_real38.59
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real5.4780e+08
I(0) uncertainty (real space) i0_real_error7.9330e+06
Rg (reciprocal space) rg_reciprocal38.79
I(0) (reciprocal space) i0_reciprocal547900000.0000
Solution quality estimate total_estimate0.8886
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.083
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha44360000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)