› 5to8

X-ray diffraction
1.98Å resolution

Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2 potency

Released:
DOI: 10.2210/pdb5to8/pdb
PDB entry 5to8 coloured by chain, front view.
PDB entry 5to8 coloured by chain, side view.
PDB entry 5to8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2 potency.
Farand J, Mai N, Chandrasekhar J, Newby ZE, Van Veldhuizen J, Loyer-Drew J, Venkataramani C, Guerrero J, Kwok A, Li N, Zherebina Y, Wilbert S, Zablocki J, Phillips G, Watkins WJ, Mourey R, Notte GT
Bioorg Med Chem Lett 26 5926-5930 (2016)
PMID: 27876318

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: 282 amino acids
Theoretical weight: 32.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14289 (Residues: 414-692; 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 7FM 1 x 7FM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 37.625Å b: 93.565Å c: 43.214Å
α: 90° β: 93.85° γ: 90°
R-values:
R R work R free
0.206 0.203 0.235
Expression system: Escherichia coli

Quick links

Citations

4 review citations

FAK inhibitors in Cancer, a patent review.
Lv et al. (2018)
3 more

3 mentions without citation

An Intriguing Purview on the Design of Macrocyclic Inhibitors for Unexplored Protein Kinases through Their Binding Site Comparison.
Bhujbal et al. (2023)
2 more