Thit with LMG135 bound

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 3% strand (DSSP).

Ligands and binding sites

• BNG · nonyl beta-D-glucopyranoside · ligand · 6 copies · chains A, B
• 2VY · 4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophene-2-carbaldehyde · ligand · 2 copies · chains A, B
• CL · Chloride ion · ion · chains B
• PEG · Di(hydroxyethyl)ether · additive · 10 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · 9 copies · chains A, B
• 1PE · Pentaethylene glycol · additive · 3 copies · chains A, B
• PGE · Triethylene glycol · additive · 3 copies · chains A, B
• PG0 · 2-(2-methoxyethoxy)ethanol · additive · 2 copies · chains A, B
• P6G · Hexaethylene glycol · additive

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 617 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 4POV · ThiT with LMG135 bound · the same entry in another collection · chain A against A, TM-score 1.00
• A2RI47 · AlphaFold monomer V2.0 prediction for thiamine transporter thit (A2RI47) · 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 A2RI47
• Elsewhere: RCSB PDB 4POV · PDBe 4POV · UniProt A2RI47