Research workbench
Crystal structure of a ternary FGF1-FGFR2-heparin complex
Analyse Crystal structure of a ternary FGF1-FGFR2-heparin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E0O
- Type
- protein
- Length
- 652 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor 1; Fibroblast growth factor receptor 2
- UniProt
- P05230, P21802
- Ligands
- SGN, IDS, NI, SO4
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor 1 | protein | 129 | 2% helix, 39% strand | P05230 |
| B | Fibroblast growth factor receptor 2 | protein | 197 | 9% helix, 52% strand | P21802 |
| C | Fibroblast growth factor 1 | protein | 130 | 7% helix, 40% strand | P05230 |
| D | Fibroblast growth factor receptor 2 | protein | 196 | 6% helix, 51% strand | P21802 |
Ligands and binding sites
- SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 5 copies · chains C, A, B
- IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · 5 copies · chains A, C, B
- NI · Nickel (II) ion · metal · 5 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 5 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.61 | 0.77 | 46 | SO4 |
| 2 | 261 | 0.60 | 0.79 | 28 | empty |
| 3 | 152 | 0.43 | 0.75 | 24 | SO4 |
| 4 | 121 | 0.40 | 0.75 | 25 | empty |
| 5 | 117 | 0.38 | 0.74 | 22 | SGN |
Interfaces
3 interfaces between chains.
- C–D · 936 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 918 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 229 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1E0O · Crystal structure of a ternary FGF1-FGFR2-heparin complex · the same entry in another collection · chain D against D, TM-score 1.00
- P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P21802 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21802) · a predicted model of the same protein · chain B against A, TM-score 0.68
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 P05230
- Every structure of UniProt P21802
- Elsewhere: RCSB PDB 1E0O · PDBe 1E0O · UniProt P05230 · UniProt P21802
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.