5D7H

X-RAY CRYSTAL STRUCTURE OF L,D TRANSPEPTIDASE 2 FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 5D7H

Entry DOI	10.2210/pdb5d7h/pdb
Descriptor	L,D-transpeptidase 2, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywords	transferase
Biological source	Mycobacterium tuberculosis
Total number of polymer chains	2
Total formula weight	77183.05
Authors	Saavedra, H.,Basta, L.A.,Lamichhane, G.,Bianchet, M.A. (deposition date: 2015-08-13, release date: 2016-09-28, Last modification date: 2024-03-06)
Primary citation	Bianchet, M.A.,Pan, Y.H.,Basta, L.A.B.,Saavedra, H.,Lloyd, E.P.,Kumar, P.,Mattoo, R.,Townsend, C.A.,Lamichhane, G. Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem. BMC Biochem., 18:8-8, 2017 Cited by PubMed Abstract: The carbapenem subclass of β-lactams is among the most potent antibiotics available today. Emerging evidence shows that, unlike other subclasses of β-lactams, carbapenems bind to and inhibit non-classical transpeptidases (L,D-transpeptidases) that generate 3 → 3 linkages in bacterial peptidoglycan. The carbapenems biapenem and tebipenem exhibit therapeutically valuable potencies against Mycobacterium tuberculosis (Mtb). PubMed: 28545389 DOI: 10.1186/s12858-017-0082-4 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.49 Å)

Structure validation