Research workbench
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
Analyse PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5X1O
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor 2
- UniProt
- P09038
- Ligands
- I3P
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fibroblast growth factor 2 | protein | 127 | 12% helix, 43% strand | P09038 |
Ligands and binding sites
- I3P · D-myo-inositol-1,4,5-triphosphate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.40 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 226 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5X1O · PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface… · the same entry in another collection · chain A against A, TM-score 1.00
- P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain B against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09038
- Elsewhere: RCSB PDB 5X1O · PDBe 5X1O · UniProt P09038
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