PDBe 1sm2

X-ray diffraction
2.3Å resolution

Crystal structure of the phosphorylated Interleukin-2 tyrosine kinase catalytic domain

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase ITK/TSK Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 30.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08881 (Residues: 357-620; Coverage: 43%)
Gene names: EMT, ITK, LYK
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: C2
Unit cell:
a: 125.1Å b: 74.4Å c: 78.9Å
α: 90° β: 93.9° γ: 90°
R-values:
R R work R free
0.246 0.214 0.292
Expression system: Escherichia coli