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Structural complex of FTO/FLUORESCEIN
Analyse Structural complex of FTO/FLUORESCEIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZS2
- Type
- protein
- Length
- 432 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
- AKG, FLU, MN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent dioxygenase fto (EC 1.14.11.-) | protein | 432 | 43% helix, 22% strand | Q9C0B1 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- FLU · 2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)-benzoic acid · ligand · chains A
- MN · Manganese (II) ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.68 | 0.82 | 41 | AKG, FLU, MN |
| 2 | 155 | 0.58 | 0.83 | 21 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9C0B1
- Elsewhere: RCSB PDB 4ZS2 · PDBe 4ZS2 · UniProt Q9C0B1
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