› 4f64

X-ray diffraction
2.05Å resolution

Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 6

Released:
DOI: 10.2210/pdb4f64/pdb
PDB entry 4f64 coloured by chain, front view.
PDB entry 4f64 coloured by chain, side view.
PDB entry 4f64 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Protein-ligand crystal structures can guide the design of selective inhibitors of the FGFR tyrosine kinase.
Norman RA, Schott AK, Andrews DM, Breed J, Foote KM, Garner AP, Ogg D, Orme JP, Pink JH, Roberts K, Rudge DA, Thomas AP, Leach AG
J Med Chem 55 5003-12 (2012)
PMID: 22612866

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor receptor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 35.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11362 (Residues: 458-765; Coverage: 39%)
Gene names: BFGFR, CEK, FGFBR, FGFR1, FLG, FLT2, HBGFR
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 0S8 2 x 0S8
Ligand EDO 4 x EDO
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2
Unit cell:
a: 208.81Å b: 57.277Å c: 65.433Å
α: 90° β: 107.55° γ: 90°
R-values:
R R work R free
0.217 0.214 0.269
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Fibroblast Growth Factor Receptors (FGFRs): Structures and Small Molecule Inhibitors.
Dai et al. (2019)
3 more

7 mentions without citation

Landscape of activating cancer mutations in FGFR kinases and their differential responses to inhibitors in clinical use.
Patani et al. (2016)
6 more