Research workbench
Disease linked mutation in fgfr
Analyse Disease linked mutation in fgfr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FLF
- Type
- protein
- Length
- 1,419 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor receptor 1
- EC
- 2.7.10.1
- UniProt
- P11362
- Ligands
- SO4, CL
- Pockets
- 17 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 296 | 36% helix, 20% strand | P11362 |
| B | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 292 | 37% helix, 18% strand | P11362 |
| C | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 283 | 38% helix, 19% strand | P11362 |
| D | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 290 | 38% helix, 18% strand | P11362 |
| E | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 258 | 40% helix, 16% strand | P11362 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D, E
- CL · Chloride ion · ion · 5 copies · chains B, C, D
- PGE · Triethylene glycol · additive · 4 copies · chains C, D
- ACT · Acetate ion · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1103 | 0.82 | 0.83 | 95 | empty |
| 2 | 1114 | 0.80 | 0.81 | 87 | CL |
| 3 | 132 | 0.57 | 0.84 | 28 | SO4 |
| 4 | 212 | 0.51 | 0.76 | 32 | empty |
| 5 | 115 | 0.50 | 0.80 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1721 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1341 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 436 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 414 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 P11362
- Elsewhere: RCSB PDB 5FLF · PDBe 5FLF · UniProt P11362
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