› 4ny0

X-ray diffraction
2.8Å resolution

Crystal structure of FERM domain of human focal adhesion kinase

Released:
DOI: 10.2210/pdb4ny0/pdb
PDB entry 4ny0 coloured by chain, front view.
PDB entry 4ny0 coloured by chain, side view.
PDB entry 4ny0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
FAK dimerization controls its kinase-dependent functions at focal adhesions.
Brami-Cherrier K, Gervasi N, Arsenieva D, Walkiewicz K, Boutterin MC, Ortega A, Leonard PG, Seantier B, Gasmi L, Bouceba T, Kadaré G, Girault JA, Arold ST
EMBO J 33 356-70 (2014)
PMID: 24480479

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170203 (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: 376 amino acids
Theoretical weight: 43.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05397 (Residues: 31-405; Coverage: 36%)
Gene names: FAK, FAK1, PTK2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 71.96Å b: 152.5Å c: 95.34Å
α: 90° β: 93.62° γ: 90°
R-values:
R R work R free
0.195 0.193 0.23
Expression system: Escherichia coli

Quick links

Citations

28 review citations

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

4 mentions without citation

FERM domain-containing proteins are active components of the cell nucleus.
Borkúti et al. (2024)
3 more