9S4H

Crystal structure of Arabidopsis thaliana Fatty Acid Thioesterase A with the x1816-FU1 ligand

This is a non-PDB format compatible entry.

Summary for 9S4H

• Entry DOI: 10.2210/pdb9s4h/pdb
• Descriptor: Oleoyl-acyl carrier protein thioesterase 1, chloroplastic, 1-(3,5-dihydro-2~{H}-1,4-benzothiazepin-4-yl)ethanone (3 entities in total)
• Functional Keywords: fatty acid thioesterase, plant, fatty acid biosynthesis, fatty acid, chain termination, dimer, hydrolase, acyl-acp thioesterase, acyl acp thioesterase, 18:1 fa, fata, acp, herbicide, mode of action
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 33822.89

Authors

Kot, E.,Ni, X.,Mulholland, N.P.,Montgomery, M.G.,von Delft, F. (deposition date: 2025-07-28, release date: 2025-08-13, Last modification date: 2026-03-04)

Primary citation

Kot, E.,Ferla, M.P.,Hollinshead, P.H.,Tomlinson, C.W.E.,Fearon, D.,Aschenbrenner, J.C.,Koekemoer, L.,Winokan, M.,Fairhead, M.,Ni, X.,Chalk, R.,England, K.S.,Varga, L.O.,Montgomery, M.G.,Mulholland, N.P.,von Delft, F.
Crystal structure of fatty acid thioesterase A bound by 129 fragments provides diverse development opportunities.
Pest Manag Sci, 82:151-168, 2026

PubMed Abstract: In order to alleviate the growing issue of herbicide resistance, diversification of the herbicide portfolio is necessary. A promising yet underutilized mode-of-action is the inhibition of fatty acid thioesterases (FATs), which terminate de novo fatty acid (FA) biosynthesis by releasing FAs from acyl carrier protein (ACP) cofactors. These enzymes impact plant growth and sterility by determining the amount and length of FAs present. In this study we report a crystallographic fragment screening approach for the identification of novel chemical matter targeting FATs.

PubMed: 40936424
DOI: 10.1002/ps.70199

Experimental method

X-RAY DIFFRACTION (2.24 Å)