8OQM
Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-10
This is a non-PDB format compatible entry.
Summary for 8OQM
Entry DOI | 10.2210/pdb8oqm/pdb |
Descriptor | 3-hydroxyacyl-CoA dehydrogenase, Putative acyltransferase Rv0859, SULFATE ION, ... (7 entities in total) |
Functional Keywords | fatty acid beta oxidation complex, mycobacterium tuberculosis, tfe, fragment screening, substrate channeling, oxidoreductase |
Biological source | Mycobacterium tuberculosis H37Rv More |
Total number of polymer chains | 4 |
Total formula weight | 244194.01 |
Authors | Dalwani, S.,Wierenga, R.K.,Venkatesan, R. (deposition date: 2023-04-12, release date: 2024-01-24, Last modification date: 2024-08-14) |
Primary citation | Dalwani, S.,Metz, A.,Huschmann, F.U.,Weiss, M.S.,Wierenga, R.K.,Venkatesan, R. Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them. Acta Crystallogr D Struct Biol, 80:605-619, 2024 Cited by PubMed: 39012716DOI: 10.1107/S2059798324006557 PDB entries with the same primary citation |
Experimental method |
Structure validation
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