4znx

Crystal structure of the Fyn-SH3 domain in complex with the high affinity peptide APP12

Method: X-RAY DIFFRACTION Dmax: 63.3 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 84–141 Chain B; UniProt 84–141 Chain C; UniProt 84–141 Chain D; UniProt 84–141 Fragment:SH3 DOMAIN, UNP residues 84-141 APP12 × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;4 M sodium formate, 0.1 M Hepes Resolution 2.10 Å R-free 0.222

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 1–58; UniProt 84–141 Author chain B; PDBConstruct 1–58; UniProt 84–141 Author chain C; PDBConstruct 1–58; UniProt 84–141 Author chain D; PDBConstruct 1–58; UniProt 84–141

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 4znx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4znx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4znx
Deposition date deposition_date2015-05-05
Structure title titleCrystal structure of the Fyn-SH3 domain in complex with the high affinity peptide APP12
Keywords keywordsbeta shandwich, 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_guinier20.11
Radius of gyration Rg (electron density) rg_electron19.14
Forward intensity I(0) i014466000.00
Molecular weight molecular_weight28966.0 kDa
Excluded volume excluded_volume36302 ų
Envelope volume envelope_volume42591 ų
Hydration-shell volume shell_volume18759 ų
Envelope diameter envelope_diameter62.9
Shell Rg shell_rg25.17
Envelope Rg envelope_rg19.07
Shape Rg shape_rg19.08
Total Rg total_rg20.24
Total atoms total_atoms3962
Residues n_residues266
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 dmax63.3
Rg (real space) rg_real20.02
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.4470e+07
I(0) uncertainty (real space) i0_real_error1.7400e+05
Rg (reciprocal space) rg_reciprocal20.04
I(0) (reciprocal space) i0_reciprocal14470000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.4
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11540000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4znxA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id4znxB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id4znxC00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id4znxD00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains

8. Citations (1)

9. Files and Curves (10)