› 5x1o

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

Released:
DOI: 10.2210/pdb5x1o/pdb
PDB 5x1o coloured by chain and viewed from the front.
PDB 5x1o coloured by chain and viewed from the side.
PDB 5x1o coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry author: Tsao YH

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand I3P 2 x I3P
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-values:
R R work R free
0.227 0.225 0.276
Expression system: Escherichia coli

Quick links