› 2hda

X-ray diffraction
1.9Å resolution

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
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-139848 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Yes Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07947 (Residues: 90-152; Coverage: 12%)
Gene names: YES, YES1
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P6322
Unit cell:
a: 46.009Å b: 46.009Å c: 90.431Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.214 0.27
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain.
Cámara-Artigas A. (2016)
1 more

8 mentions without citation

Protein 3D structure computed from evolutionary sequence variation.
Marks et al. (2011)
7 more