› 2jko

X-ray diffraction
1.65Å resolution

Focal Adhesion Kinase catalytic domain in complex with bis-anilino pyrimidine inhibitor

Released:
DOI: 10.2210/pdb2jko/pdb
PDB entry 2jko coloured by chain, front view.
PDB entry 2jko coloured by chain, side view.
PDB entry 2jko coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation.
Lietha D, Eck MJ
PLoS One 3 e3800 (2008)
PMID: 19030106

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-169484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Focal adhesion kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 31.73 KDa
Source organism: Gallus gallus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q00944 (Residues: 411-686; Coverage: 26%)
Gene names: FAK, FAK1, PTK2
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 45.691Å b: 47.063Å c: 62.979Å
α: 90° β: 98.63° γ: 90°
R-values:
R R work R free
0.19 0.188 0.217
Expression system: Trichoplusia ni

Quick links

Citations

13 review citations

FAK in cancer: mechanistic findings and clinical applications.
Sulzmaier et al. (2014)
12 more

2 mentions without citation

Exploring Ligand Stability in Protein Crystal Structures Using Binding Pose Metadynamics.
Fusani et al. (2020)
1 more