› 4nka

X-ray diffraction
2.19Å resolution

Crystal structure of human fibroblast growth factor receptor 1 kinase domain in complex with pyrazolaminopyrimidine 2

Released:
DOI: 10.2210/pdb4nka/pdb
PDB entry 4nka coloured by chain, front view.
PDB entry 4nka coloured by chain, side view.
PDB entry 4nka coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
FGFR1 Kinase Inhibitors: Close Regioisomers Adopt Divergent Binding Modes and Display Distinct Biophysical Signatures.
Klein T, Tucker J, Holdgate GA, Norman RA, Breeze AL
ACS Med Chem Lett 5 166-71 (2014)
PMID: 24900792

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 SO4 3 x SO4
Ligand EDO 3 x EDO
Ligand 2K7 2 x 2K7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 208.83Å b: 57.36Å c: 65.73Å
α: 90° β: 107.68° γ: 90°
R-values:
R R work R free
0.2 0.198 0.228
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Functional proteomics of the epigenetic regulators ASXL1, ASXL2 and ASXL3: a convergence of proteomics and epigenetics for translational medicine.
Katoh M. (2015)
3 other articles

2 mentions without citation

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