1djs

X-ray diffraction
2.4Å resolution

LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1

Released:
Source organism: Homo sapiens
Primary publication:
Structural interactions of fibroblast growth factor receptor with its ligands.
Proc Natl Acad Sci U S A 97 49-54 (2000)
PMID: 10618369

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-138611 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fibroblast growth factor receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 24.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21802 (Residues: 151-362; Coverage: 27%)
Gene names: BEK, FGFR2, KGFR, KSAM
Sequence domains:
Structure domains: Immunoglobulins
Fibroblast growth factor 1 Chain: B
Molecule details ›
Chain: B
Length: 135 amino acids
Theoretical weight: 15.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05230 (Residues: 21-155; Coverage: 87%)
Gene names: FGF1, FGFA
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: I422
Unit cell:
a: 129.97Å b: 129.97Å c: 129.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.221 0.315
Expression system: Escherichia coli