5NGZ

Ube2T in complex with fragment EM04

Summary for 5NGZ

• Entry DOI: 10.2210/pdb5ngz/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 T, 1-(1,3-benzothiazol-2-yl)methanamine (3 entities in total)
• Functional Keywords: ubiquitin-conjugating enzyme ube2t, fragment screening, fanconi anemia pathway, dna repair, ligase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : Q9NPD8
• Total number of polymer chains: 1
• Total formula weight: 22718.10

Authors

Morreale, F.E.,Bortoluzzi, A.,Chaugule, V.K.,Arkinson, C.,Walden, H.,Ciulli, A. (deposition date: 2017-03-21, release date: 2017-05-03, Last modification date: 2024-01-17)

Primary citation

Morreale, F.E.,Bortoluzzi, A.,Chaugule, V.K.,Arkinson, C.,Walden, H.,Ciulli, A.
Allosteric Targeting of the Fanconi Anemia Ubiquitin-Conjugating Enzyme Ube2T by Fragment Screening.
J. Med. Chem., 60:4093-4098, 2017

PubMed Abstract: Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway and it is overexpressed in several cancers, representing an attractive target for the development of inhibitors. Despite the extensive efforts in targeting the ubiquitin system, very few E2 binders have currently been discovered. Herein we report the identification of a new allosteric pocket on Ube2T through a fragment screening using biophysical methods. Several fragments binding to this site inhibit ubiquitin conjugation in vitro.

PubMed: 28437106
DOI: 10.1021/acs.jmedchem.7b00147

Experimental method

X-RAY DIFFRACTION (2.4 Å)