› 2psq

X-ray diffraction
2.4Å resolution

Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain

Released:
DOI: 10.2210/pdb2psq/pdb
PDB entry 2psq coloured by chain, front view.
PDB entry 2psq coloured by chain, side view.
PDB entry 2psq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.
Chen H, Ma J, Li W, Eliseenkova AV, Xu C, Neubert TA, Miller WT, Mohammadi M
Mol Cell 27 717-30 (2007)
PMID: 17803937

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 42.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21802 (Residues: 413-768; Coverage: 45%)
Gene names: BEK, FGFR2, KGFR, KSAM
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 106.61Å b: 118.605Å c: 63.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.258
Expression system: Escherichia coli

Quick links

Citations

42 review citations

Cell signaling by receptor tyrosine kinases.
Lemmon et al. (2010)
41 more

22 mentions without citation

Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology.
Belov et al. (2013)
21 more