› 5flf

X-ray diffraction
2.58Å 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, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 310 amino acids
Theoretical weight: 35.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

4 bound ligands:
Ligand SO4 9 x SO4
Ligand ACT 1 x ACT
Ligand CL 5 x CL
Ligand PGE 4 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 76.259Å b: 152.281Å c: 195.887Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Achondroplasia: Development, pathogenesis, and therapy.
Ornitz et al. (2017)
16 more

1 mention without citation

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