Research workbench
Native FGFR1 with an inhibitor
Analyse Native FGFR1 with an inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AM6
- Type
- protein
- Length
- 575 residues
- Chains
- 2
- 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
- 38O, CL
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 295 | 38% helix, 14% strand | P11362 |
| B | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 280 | 40% helix, 16% strand | P11362 |
Ligands and binding sites
- 38O · 4-amino-5-fluoro-3-[5-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]quinolin-2(1H)-one · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.70 | 0.77 | 58 | CL, 38O |
| 2 | 380 | 0.67 | 0.80 | 38 | 38O |
| 3 | 458 | 0.64 | 0.77 | 57 | empty |
| 4 | 108 | 0.44 | 0.78 | 23 | CL |
Interfaces
1 interface between chains.
- A–B · 511 Ų buried · 10 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 5AM6 · PDBe 5AM6 · UniProt P11362
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