Research workbench
Crystal structure of the human fat mass and obesity associated protein (fto) in complex with citrate and rhein (rhn)
Analyse Crystal structure of the human fat mass and obesity associated protein (fto) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IE7
- Type
- protein
- Length
- 439 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
- RHN, ZN
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent dioxygenase fto (EC 1.14.11.-) | protein | 439 | 40% helix, 22% strand | Q9C0B1 |
Ligands and binding sites
- RHN · 4,5-dihydroxy-9,10-dioxo-9,10-dihydroanthracene-2-carboxylic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.70 | 0.84 | 38 | RHN, FLC |
| 2 | 82 | 0.31 | 0.73 | 20 | empty |
| 3 | 52 | 0.31 | 0.77 | 13 | empty |
| 4 | 50 | 0.25 | 0.72 | 12 | empty |
Compared structures
- 4IE7 · Crystal structure of the human fat mass and obesity associated protein (FTO) in complex… · 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 4IE7 · PDBe 4IE7 · UniProt Q9C0B1
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