Research workbench
Human FGF in complex with a covalent inhibitor
Analyse Human FGF in complex with a covalent inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O49
- 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
- 9K5, SO4
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 289 | 38% helix, 16% strand | P11362 |
| B | Fibroblast growth factor receptor 1 (EC 2.7.10.1) | protein | 286 | 38% helix, 16% strand | P11362 |
Ligands and binding sites
- 9K5 · [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl 3-fluorosulfonylbenzoate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 771 | 0.73 | 0.78 | 78 | empty |
| 2 | 692 | 0.70 | 0.77 | 60 | 9K5 |
| 3 | 382 | 0.65 | 0.79 | 34 | 9K5 |
| 4 | 87 | 0.41 | 0.78 | 18 | empty |
| 5 | 73 | 0.32 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 398 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 5O49 · PDBe 5O49 · UniProt P11362
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.