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7WT0

human glyoxalase I (with C-ter His tag) in complex with TLSC702

Summary for 7WT0
Entry DOI10.2210/pdb7wt0/pdb
DescriptorLactoylglutathione lyase, ZINC ION, (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid, ... (4 entities in total)
Functional Keywordsglyoxalase i, zinc metalloenzyme, lyase
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight44531.32
Authors
Usami, M.,Yokoyama, H. (deposition date: 2022-02-03, release date: 2022-04-13, Last modification date: 2023-11-29)
Primary citationUsami, M.,Ando, K.,Shibuya, A.,Takasawa, R.,Yokoyama, H.
Crystal structures of human glyoxalase I and its complex with TLSC702 reveal inhibitor binding mode and substrate preference.
Febs Lett., 596:1458-1467, 2022
Cited by
PubMed Abstract: Human glyoxalase I (hGLO I) is an enzyme for detoxification of methylglyoxal (MG) and has been considered an attractive target for the development of new anticancer drugs. In our previous report, the GLO I inhibitor TLSC702 induced apoptosis in tumor cells. Here, we determined the crystal structures of hGLO I and its complex with TLSC702. In the complex, the carboxyl O atom of TLSC702 is coordinated to Zn , and TLSC702 mainly shows van der Waals interaction with hydrophobic residues. In the inhibitor-unbound structure, glycerol, which has similar functional groups to MG, was bound to Zn , indicating that GLO I can easily bind to MG. This study provides a structural basis to develop better anticancer drugs.
PubMed: 35363883
DOI: 10.1002/1873-3468.14344
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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