3ua6

X-ray diffraction
1.85Å resolution

Crystal Structure of the Human Fyn SH3 domain

Released:
Source organism: Homo sapiens
Primary publication:
The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein.
Acta Crystallogr D Biol Crystallogr 68 1030-40 (2012)
PMID: 22868769

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Fyn Chains: A, B
Molecule details ›
Chains: A, B
Length: 64 amino acids
Theoretical weight: 7.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06241 (Residues: 81-143; Coverage: 12%)
Gene name: FYN
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2
Unit cell:
a: 72.293Å b: 47.074Å c: 42.467Å
α: 90° β: 98.52° γ: 90°
R-values:
R R work R free
0.18 0.177 0.246
Expression system: Escherichia coli BL21(DE3)