3ua7

X-ray diffraction
1.5Å resolution

Crystal Structure of the Human Fyn SH3 domain in complex with a peptide from the Hepatitis C virus NS5A-protein

Released:
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

Reactions catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-138963 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase Fyn Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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
Non-structural protein 5A Chains: E, F
Molecule details ›
Chains: E, F
Length: 12 amino acids
Theoretical weight: 1.31 KDa
Source organism: Hepacivirus hominis
Expression system: Not provided
UniProt:
  • Canonical: P26663 (Residues: 2321-2331; Coverage: 0%)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 51.39Å b: 51.39Å c: 185.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.185 0.231
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided