8EVN
Sulfatase from Mycobacterium tuberculosis (Rv3406) in complex with N-oxalylglycine (NOG)
Summary for 8EVN
| Entry DOI | 10.2210/pdb8evn/pdb |
| Related | 4FFA |
| Descriptor | Alpha-ketoglutarate-dependent sulfate ester dioxygenase, N-OXALYLGLYCINE, NICKEL (II) ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase-inhibitor complex, sulfatase, 2-oxoglutarate dependent dioxygenase, oxidoreductase/inhibitor |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 4 |
| Total formula weight | 132549.81 |
| Authors | Juan, T.-J.,Leung, I.,Squire, C.J. (deposition date: 2022-10-20, release date: 2023-10-25, Last modification date: 2026-03-18) |
| Primary citation | Juan, V.T.,Bajan, P.,Eurtivong, C.,Liu, T.,Squire, C.J.,Huang, E.Y.,Leung, I.K.H. Structural remodelling of the 2OG oxygenase Rv3406 enables sulfur-scavenging in Mycobacterium tuberculosis. Chem.Commun.(Camb.), 61:19020-19023, 2025 Cited by PubMed Abstract: Rv3406 evolved from the ubiquitous taurine-catabolising enzyme TauD and functions as a sulfur-scavenging protein in . Structural and biochemical analyses reveal specific changes that shape its chemical environment for ligand interaction and explain its broad substrate range. These findings show how amino acid substitutions redefine protein function and drive adaptation to the unique metabolic context of Mycobacteria. PubMed: 41178574DOI: 10.1039/d5cc05573c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.644 Å) |
Structure validation
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