9ghk

Crystal structure of Fyn SH3 domain/tau 214-220 peptide complex

Method: X-RAY DIFFRACTION Dmax: 53.3 Å Quality: GOOD

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

Isoform 2 of 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 80–143 Chain B; UniProt 80–143 Not recorded Tau peptide ARG-THR-PRO-SER-LEU-PRO-THR-PRO-PRO-THR × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M NaCl, 0.4 M NaH2PO4, 1.5 M K2HPO4, 0.1 M imidazole pH 7.5 Resolution 1.42 Å R-free 0.218

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 P06241-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–64; UniProt 80–143 Author chain B; PDBConstruct 1–64; UniProt 80–143

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 9ghk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ghk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ghk
Deposition date deposition_date2024-08-15
最后修订 last_revision2025-08-27
Structure title titleCrystal structure of Fyn SH3 domain/tau 214-220 peptide complex
Keywords keywordsFyn SH3 domain, proline-rich region of Tau, heterotrimeric Fyn SH3-tau peptide complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.13
Radius of gyration Rg (electron density) rg_electron14.80
Forward intensity I(0) i03863350.00
Molecular weight molecular_weight14098.0 kDa
Excluded volume excluded_volume17612 ų
Envelope volume envelope_volume19707 ų
Hydration-shell volume shell_volume11711 ų
Envelope diameter envelope_diameter51.8
Shell Rg shell_rg19.92
Envelope Rg envelope_rg15.08
Shape Rg shape_rg14.75
Total Rg total_rg15.96
Total atoms total_atoms1001
Residues n_residues126
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 dmax53.3
Rg (real space) rg_real16.12
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.8630e+06
I(0) uncertainty (real space) i0_real_error4.6510e+04
Rg (reciprocal space) rg_reciprocal16.12
I(0) (reciprocal space) i0_reciprocal3863000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.6
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1174000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)