X-ray diffraction
1.9Å resolution

PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study

Source organism: Homo sapiens
Entry author: Tsao YH

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Fibroblast growth factor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P09038 (Residues: 143-288; Coverage: 51%)
Gene names: FGF2, FGFB
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P212121
Unit cell:
a: 34.616Å b: 67.346Å c: 122.196Å
α: 90° β: 90° γ: 90°
R R work R free
0.227 0.225 0.276
Expression system: Escherichia coli