› 2jkk

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb2jkk/pdb
PDB entry 2jkk coloured by chain, front view.
PDB entry 2jkk coloured by chain, side view.
PDB entry 2jkk 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

2 bound ligands:
Ligand SO4 1 x SO4
Ligand BI9 1 x BI9
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 44.135Å b: 45.153Å c: 67.457Å
α: 90° β: 94.7° γ: 90°
R-values:
R R work R free
0.182 0.179 0.236
Expression system: Trichoplusia ni

Quick links

Citations

10 review citations

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

17 mentions without citation

Drug Discovery Targeting Focal Adhesion Kinase (FAK) as a Promising Cancer Therapy.
Pang et al. (2021)
16 more