› 6yxv

X-ray diffraction
2.3Å resolution

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-Methyl-N-{3-[(2-phenylamino-5-trifluoromethyl-pyrimidin-4-ylamino)-methyl]-pyridin-2-yl}-methanesulfonamide

Released:
DOI: 10.2210/pdb6yxv/pdb
PDB entry 6yxv coloured by chain, front view.
PDB entry 6yxv coloured by chain, side view.
PDB entry 6yxv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2.
Berger BT, Amaral M, Kokh DB, Nunes-Alves A, Musil D, Heinrich T, Schröder M, Neil R, Wang J, Navratilova I, Bomke J, Elkins JM, Müller S, Frech M, Wade RC, Knapp S
Cell Chem Biol 28 686-698.e7 (2021)
PMID: 33497606

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-170202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Focal adhesion kinase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 282 amino acids
Theoretical weight: 32.3 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q05397 (Residues: 411-689; Coverage: 27%)
Gene names: FAK, FAK1, PTK2
Sequence domains: Protein tyrosine and serine/threonine kinase

Ligands and Environments

2 bound ligands:
Ligand Q2H 4 x Q2H
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 118.05Å b: 77.127Å c: 174.934Å
α: 90° β: 101.34° γ: 90°
R-values:
R R work R free
0.204 0.202 0.232
Expression system: Trichoplusia ni

Quick links

Citations

2 review citations

Trends in kinase drug discovery: targets, indications and inhibitor design.
Attwood et al. (2021)
1 more

1 mention without citation

Interactions between curcumin and human salt-induced kinase 3 elucidated from computational tools and experimental methods.
Shi et al. (2023)