Research workbench
Crystal structure of FGFR4 kinase domain in complex with a covalent inhibitor
Analyse Crystal structure of FGFR4 kinase domain 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
- 6IUO
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Fibroblast growth factor receptor 4
- EC
- 2.7.10.1
- UniProt
- P22455
- Ligands
- AWX
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · resolution 2.3 · 1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 4 (EC 2.7.10.1) | protein | 275 | 41% helix, 14% strand | P22455 |
Ligands and binding sites
- AWX · N-({4-[4-amino-3-(3,5-dimethyl-1-benzofuran-2-yl)-7-oxo-6,7-dihydro-2H-pyrazolo[3,4-d]pyridazin-2-yl]phenyl}methyl)prop-2-enamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.62 | 0.80 | 30 | AWX |
| 2 | 65 | 0.32 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6IUO · Crystal structure of FGFR4 kinase domain in complex with a covalent inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P22455 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 4 (P22455) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P22455
- Elsewhere: RCSB PDB 6IUO · PDBe 6IUO · UniProt P22455
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