6SBU
X-ray Structure of Human LDHA with an Allosteric Inhibitor (Compound 3)
Summary for 6SBU
| Entry DOI | 10.2210/pdb6sbu/pdb |
| Descriptor | L-lactate dehydrogenase A chain, 4-[[4-[(5-chloranylthiophen-2-yl)carbonylamino]-1,3-bis(oxidanylidene)isoindol-2-yl]methyl]benzoic acid, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | ldha, oxidoreductase, oxidoreductase inhibitor, allosteric inhibitor |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 8 |
| Total formula weight | 298141.95 |
| Authors | Friberg, A.,Puetter, V.,Nguyen, D.,Rehwinkel, H. (deposition date: 2019-07-22, release date: 2020-06-10, Last modification date: 2024-01-24) |
| Primary citation | Friberg, A.,Rehwinkel, H.,Nguyen, D.,Putter, V.,Quanz, M.,Weiske, J.,Eberspacher, U.,Heisler, I.,Langer, G. Structural Evidence for Isoform-Selective Allosteric Inhibition of Lactate Dehydrogenase A. Acs Omega, 5:13034-13041, 2020 Cited by PubMed Abstract: Lactate dehydrogenase A (LDHA) is frequently overexpressed in tumors, thereby sustaining high glycolysis rates, tumor growth, and chemoresistance. High-throughput screening resulted in the identification of phthalimide and dibenzofuran derivatives as novel lactate dehydrogenase inhibitors, selectively inhibiting the activity of the LDHA isoenzyme. Cocrystallization experiments confirmed target engagement in addition to demonstrating binding to a novel allosteric binding site present in all four LDHA subunits of the LDH5 homotetramer. PubMed: 32548488DOI: 10.1021/acsomega.0c00715 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.91 Å) |
Structure validation
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