› 5a4c

X-ray diffraction
2.09Å resolution

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-145801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor receptor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 34.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11362 (Residues: 461-765; Coverage: 38%)
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 6 x SO4
Ligand EDO 10 x EDO
Ligand XOJ 2 x XOJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 208.43Å b: 57.46Å c: 65.67Å
α: 90° β: 107.34° γ: 90°
R-values:
R R work R free
0.196 0.194 0.235
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Kinetics for Drug Discovery: an industry-driven effort to target drug residence time.
Schuetz et al. (2017)
4 more

3 mentions without citation

Structural and dynamic insights into the energetics of activation loop rearrangement in FGFR1 kinase.
Klein et al. (2015)
2 more