› 3fzs

X-ray diffraction
1.75Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-tyrosine kinase 2-beta Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 32.19 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q14289 (Residues: 416-692; Coverage: 28%)
Gene names: FAK2, PTK2B, PYK2, RAFTK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand B96 1 x B96
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 37.503Å b: 81.694Å c: 87.256Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.224

Quick links

Citations

12 review citations

Therapeutic potential and limitations of new FAK inhibitors in the treatment of cancer.
Schultze et al. (2010)
11 more

5 mentions without citation

Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design.
Han et al. (2009)
4 more