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8OQV

Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-109

Summary for 8OQV
Entry DOI10.2210/pdb8oqv/pdb
Descriptor3-hydroxyacyl-CoA dehydrogenase, Putative acyltransferase Rv0859, GLYCEROL, ... (6 entities in total)
Functional Keywordsfatty acid beta oxidation complex, mycobacterium tuberculosis, tfe, fragment screening, substrate channeling, oxidoreductase
Biological sourceMycobacterium tuberculosis H37Rv
More
Total number of polymer chains4
Total formula weight244171.79
Authors
Dalwani, S.,Wierenga, R.K.,Venkatesan, R. (deposition date: 2023-04-12, release date: 2024-01-24, Last modification date: 2024-07-24)
Primary citationDalwani, 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, 2024
Cited by
PubMed: 39012716
DOI: 10.1107/S2059798324006557
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.78 Å)
Structure validation

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