Research workbench
Crystal structure of FGF1 in complex with the extracellular ligand binding domain of FGF receptor 1 (FGFR1)
Analyse Crystal structure of FGF1 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
- 1EVT
- Type
- protein
- Length
- 645 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (fibroblast growth factor 1); Protein (fibroblast growth factor receptor 1)
- UniProt
- P05230, P11362
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (fibroblast growth factor 1) | protein | 131 | 2% helix, 42% strand | P05230 |
| C | Protein (fibroblast growth factor receptor 1) | protein | 191 | 9% helix, 51% strand | P11362 |
| D | Protein (fibroblast growth factor receptor 1) | protein | 192 | 9% helix, 52% strand | P11362 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.49 | 0.75 | 32 | empty |
| 2 | 120 | 0.40 | 0.75 | 21 | empty |
| 3 | 103 | 0.39 | 0.76 | 15 | empty |
| 4 | 94 | 0.39 | 0.76 | 16 | empty |
| 5 | 92 | 0.36 | 0.75 | 16 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1154 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 1135 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1088 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 49 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 45 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1EVT · Crystal structure of FGF1 in complex with the extracellular ligand binding domain of FGF… · 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 B against A, TM-score 0.98
- P11362 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 1 (P11362) · a predicted model of the same protein · chain C against A, TM-score 0.57
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 P11362
- Elsewhere: RCSB PDB 1EVT · PDBe 1EVT · UniProt P05230 · UniProt P11362
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