7WT2
human glyoxalase I in complex with TLSC702
Summary for 7WT2
| Entry DOI | 10.2210/pdb7wt2/pdb |
| Descriptor | Lactoylglutathione lyase, ZINC ION, (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid, ... (4 entities in total) |
| Functional Keywords | glyoxalase i, zinc metalloenzyme, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 42389.01 |
| Authors | Usami, M.,Yokoyama, H. (deposition date: 2022-02-03, release date: 2022-04-13, Last modification date: 2023-11-29) |
| Primary citation | Usami, 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: 35363883DOI: 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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