3ZG4
NMR structure of the catalytic domain from E. faecium L,D- transpeptidase
Summary for 3ZG4
Entry DOI | 10.2210/pdb3zg4/pdb |
Related | 3ZGP |
NMR Information | BMRB: 18900 |
Descriptor | ERFK/YBIS/YCFS/YNHG (1 entity in total) |
Functional Keywords | transferase, transpeptidation, peptidoglycan biosynthesis, antibiotic resistance |
Biological source | ENTEROCOCCUS FAECIUM |
Total number of polymer chains | 1 |
Total formula weight | 14572.15 |
Authors | Lecoq, L.,Dubee, V.,Triboulet, S.,Bougault, C.,Hugonnet, J.E.,Arthur, M.,Simorre, J.P. (deposition date: 2012-12-14, release date: 2013-04-24, Last modification date: 2024-06-19) |
Primary citation | Lecoq, L.,Dubee, V.,Triboulet, S.,Bougault, C.,Hugonnet, J.E.,Arthur, M.,Simorre, J.P. The Structure of Enterococcus Faecium L,D---Transpeptidase Acylated by Ertapenem Provides Insight Into the Inactivation Mechanism. Acs Chem.Biol., 8:1140-, 2013 Cited by PubMed: 23574509DOI: 10.1021/CB4001603 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report