Research workbench

Structural complex of fto bound with DAC51

Analyse Structural complex of fto bound with DAC51 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CKK
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9C0B1
Ligands: OGA, B6C

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	424	—	Q9C0B1

Ligands and binding sites

OGA · N-oxalylglycine · ligand · chains A
B6C · 2-{[2,6-dichloro-4-(3,5-dimethyl-1H-pyrazol-4-yl) phenyl]amino}-N-hydroxybenzamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7CKK · Structural complex of FTO bound with Dac51 · 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 0.99

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 7CKK · PDBe 7CKK · UniProt Q9C0B1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.