7a2q

Crystal structure of the Fyn SH3 domain L112V-S114N-S115T-E121L-R123H mutant at pH 3.0 with PEG

Method: X-RAY DIFFRACTION Dmax: 38.4 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 83–143 Mutation:L112V S114N S115T E121L R123H PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;298 K;5% PEG 300, 5 mM beta-cyclodextrin, 2.0 ammonium sulfate, 0.1M sodium citrate Resolution 0.94 Å R-free 0.161

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 68 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 1–61; UniProt 83–143

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 7a2q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7a2q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7a2q
Deposition date deposition_date2020-08-18
Structure title titleCrystal structure of the Fyn SH3 domain L112V-S114N-S115T-E121L-R123H mutant at pH 3.0 with PEG
Keywords keywordsbeta barrel, SH3 domain, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier11.87
Radius of gyration Rg (electron density) rg_electron10.36
Forward intensity I(0) i01024170.00
Molecular weight molecular_weight6732.0 kDa
Excluded volume excluded_volume8420 ų
Envelope volume envelope_volume9220 ų
Hydration-shell volume shell_volume7759 ų
Envelope diameter envelope_diameter35.7
Shell Rg shell_rg15.77
Envelope Rg envelope_rg10.74
Shape Rg shape_rg10.29
Total Rg total_rg12.03
Total atoms total_atoms913
Residues n_residues58
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 dmax38.4
Rg (real space) rg_real11.79
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.0240e+06
I(0) uncertainty (real space) i0_real_error1.0420e+04
Rg (reciprocal space) rg_reciprocal11.80
I(0) (reciprocal space) i0_reciprocal1024000.0000
Solution quality estimate total_estimate0.8754
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.6
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha242900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)