9HJD

Cryo-EM structure of domperidone-bound human SLC19A3 in inward-open state

Summary for 9HJD

Entry DOI	10.2210/pdb9hjd/pdb
EMDB information	52213
Descriptor	Nb3.3, Thiamine transporter 2, Domperidone, ... (4 entities in total)
Functional Keywords	thiamine transporter, drug interaction, thiamine deficiency, membrane protein
Biological source	Lama glama More
Total number of polymer chains	2
Total formula weight	75540.51
Authors	Gabriel, F.,Loew, C. (deposition date: 2024-11-28, release date: 2025-07-30, Last modification date: 2025-12-03)
Primary citation	Gabriel, F.,Windshugel, B.,Low, C. Structure-based discovery of thiamine uptake inhibitors. Br.J.Pharmacol., 182:5611-5626, 2025 Cited by PubMed Abstract: Thiamine (vitamin B) is an essential coenzyme and catalyses various reactions in central metabolic pathways. Since mammals have lost the ability to synthesise thiamine de novo, this micronutrient has to be imported via the high affinity solute carriers SLC19A2 and A3 across the plasma membrane. Perturbations of these transport systems have severe effects on human health. Recent structural work on SLC19A2 and A3 have provided molecular insights into substrate and drug recognition and conformational changes during transport. Based on the analysis of the available SLC19A3 structures, we hypothesise that the binding site is rather promiscuous, allowing different small molecules to interact and potentially inhibit this transporter. PubMed: 40702645 DOI: 10.1111/bph.70133 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (3.35 Å)

Structure validation