Research workbench
Crystal structure of FGF2 in complex with the extracellular ligand binding domain of FGF receptor 2 (FGFR2)
Analyse Crystal structure of FGF2 in complex with the extracellular ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EV2
- Type
- protein
- Length
- 1,310 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (fibroblast growth factor 2); Protein (fibroblast growth factor receptor 2)
- UniProt
- P09038, P21802
- Ligands
- SO4
- Pockets
- 14 · best druggability 0.74
Structure
x-ray diffraction · 5 distinct chains · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Protein (fibroblast growth factor 2) | protein | 130 | 2% helix, 42% strand | P09038 |
| E | Protein (fibroblast growth factor receptor 2) | protein | 194 | 8% helix, 51% strand | P21802 |
| F | Protein (fibroblast growth factor receptor 2) | protein | 195 | 8% helix, 50% strand | P21802 |
| G | Protein (fibroblast growth factor receptor 2) | protein | 200 | 8% helix, 52% strand | P21802 |
| H | Protein (fibroblast growth factor receptor 2) | protein | 201 | 8% helix, 52% strand | P21802 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 832 | 0.74 | 0.78 | 99 | empty |
| 2 | 464 | 0.58 | 0.74 | 30 | empty |
| 3 | 276 | 0.58 | 0.78 | 39 | empty |
| 4 | 366 | 0.58 | 0.76 | 51 | empty |
| 5 | 332 | 0.56 | 0.75 | 48 | empty |
Interfaces
13 interfaces between chains.
- A–E · 1401 Ų buried · 20 hydrogen bonds · protein-protein
- C–G · 1399 Ų buried · 19 hydrogen bonds · protein-protein
- D–H · 1397 Ų buried · 19 hydrogen bonds · protein-protein
- B–F · 1386 Ų buried · 16 hydrogen bonds · protein-protein
- E–H · 874 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1EV2 · Crystal structure of FGF2 in complex with the extracellular ligand binding domain of FGF… · the same entry in another collection · chain H against H, TM-score 1.00
- P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain D 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
- Every structure of UniProt P21802
- Elsewhere: RCSB PDB 1EV2 · PDBe 1EV2 · UniProt P09038 · UniProt P21802
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