3ZGP
NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem
Summary for 3ZGP
Entry DOI | 10.2210/pdb3zgp/pdb |
Related | 3ZG4 |
NMR Information | BMRB: 18911 |
Descriptor | ERFK/YBIS/YCFS/YNHG, (4R,5S)-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid (2 entities in total) |
Functional Keywords | transferase, transpeptidation, peptidoglycan biosynthesis, antibiotic resistance |
Biological source | ENTEROCOCCUS FAECIUM |
Total number of polymer chains | 1 |
Total formula weight | 15049.68 |
Authors | Lecoq, L.,Triboulet, S.,Dubee, V.,Bougault, C.,Hugonnet, J.E.,Arthur, M.,Simorre, J.P. (deposition date: 2012-12-18, release date: 2013-04-24, Last modification date: 2023-06-14) |
Primary citation | Lecoq, L.,Triboulet, S.,Dubee, V.,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., 8:1140-1146, 2013 Cited by PubMed: 23574509DOI: 10.1021/cb4001603 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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