5X79

Human GST Pi conjugated with novel inhibitor, GS-ESF

Summary for 5X79

• Entry DOI: 10.2210/pdb5x79/pdb
• Descriptor: Glutathione S-transferase P, (2S)-2-azanyl-5-[[(2R)-3-(2-fluorosulfonylethylsulfanyl)-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: gstp, covalent inhibitor, transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : P09211
• Total number of polymer chains: 2
• Total formula weight: 47980.88

Authors

Tomoike, F.,Shishido, Y.,Fukui, K.,Kimura, Y.,Abe, H. (deposition date: 2017-02-24, release date: 2017-09-13, Last modification date: 2025-09-17)

Primary citation

Shishido, Y.,Tomoike, F.,Kimura, Y.,Kuwata, K.,Yano, T.,Fukui, K.,Fujikawa, H.,Sekido, Y.,Murakami-Tonami, Y.,Kameda, T.,Shuto, S.,Abe, H.
A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1).
Chem. Commun. (Camb.), 53:11138-11141, 2017

PubMed Abstract: We herein report the first covalent G-site-binding inhibitor for GST, GS-ESF (1), which irreversibly inhibited the GSTP function. LC-MS/MS and X-ray structure analyses of the covalently linked GST-inhibitor complex suggested that 1 reacted with Tyr108 of GSTP. The mechanism of covalent bond formation was discussed based on MD simulation results.

PubMed: 28848941
DOI: 10.1039/c7cc05829b

Experimental method

X-RAY DIFFRACTION (1.9 Å)