Research workbench
Crystal structure of fto bound to a selective inhibitor
Analyse Crystal structure of fto bound to a selective inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QKN
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-ketoglutarate-dependent dioxygenase fto
- EC
- 1.14.11.-
- UniProt
- Q9C0B1
- Ligands
- OGA, JMS, MN
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent dioxygenase fto (EC 1.14.11.-) | protein | 434 | 42% helix, 21% strand | Q9C0B1 |
Ligands and binding sites
- OGA · N-oxalylglycine · ligand · chains A
- JMS · 2-[(2,6-dichloro-3-methyl-phenyl)amino]benzoic acid · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.66 | 0.82 | 38 | OGA, JMS, MN, GOL |
| 2 | 52 | 0.31 | 0.77 | 14 | empty |
| 3 | 65 | 0.28 | 0.73 | 19 | empty |
Compared structures
- 4QKN · Crystal structure of FTO bound to a selective inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C0B1 · AlphaFold monomer V2.0 prediction for alpha-ketoglutarate-dependent dioxygenase fto… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q9C0B1
- Elsewhere: RCSB PDB 4QKN · PDBe 4QKN · UniProt Q9C0B1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.