Research workbench
Structural analysis of the human Fibroblast Growth Factor Receptor 4 Kinase
Analyse Structural analysis of the human Fibroblast Growth Factor Receptor 4 Kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TYJ
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.45
- Source
- Homo sapiens
- Molecule
- Fibroblast growth factor receptor 4
- EC
- 2.7.10.1
- UniProt
- P22455
- Ligands
- 0LI, PO4
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · resolution 2.45 · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 4 (EC 2.7.10.1) | protein | 278 | 43% helix, 16% strand | P22455 |
Ligands and binding sites
- 0LI · 3-(imidazo[1,2-b]pyridazin-3-ylethynyl)-4-methyl-N-{4-[(4-methylpiperazin-1-yl)methyl]-3-(trifluoromethyl) phenyl}benzamide · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.70 | 0.81 | 56 | 0LI |
Compared structures
- 4TYJ · Structural analysis of the human fibroblast growth factor receptor 4 kinase · 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 0.95
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 4TYJ · PDBe 4TYJ · UniProt P22455
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