6RLG
Crystal structure of LdtMt2 from Mycobacterium tuberculosis
Summary for 6RLG
| Entry DOI | 10.2210/pdb6rlg/pdb |
| Descriptor | L,D-transpeptidase 2, NITRATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total) |
| Functional Keywords | beta lactmase, antibiotic resistance, tuberculosis, antimicrobial protein |
| Biological source | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Total number of polymer chains | 2 |
| Total formula weight | 77245.58 |
| Authors | Brem, J.,Lohans, C.,Schofield, C. (deposition date: 2019-05-02, release date: 2019-08-14, Last modification date: 2024-01-24) |
| Primary citation | de Munnik, M.,Lohans, C.T.,Lang, P.A.,Langley, G.W.,Malla, T.R.,Tumber, A.,Schofield, C.J.,Brem, J. Targeting the Mycobacterium tuberculosis transpeptidase LdtMt2with cysteine-reactive inhibitors including ebselen. Chem.Commun.(Camb.), 55:10214-10217, 2019 Cited by PubMed Abstract: The l,d-transpeptidases (Ldts) are promising antibiotic targets for treating tuberculosis. We report screening of cysteine-reactive inhibitors against LdtMt2 from Mycobacterium tuberculosis. Structural studies on LdtMt2 with potent inhibitor ebselen reveal opening of the benzisoselenazolone ring by a nucleophilic cysteine, forming a complex involving extensive hydrophobic interactions with a substrate-binding loop. PubMed: 31380528DOI: 10.1039/c9cc04145a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51000183032 Å) |
Structure validation
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