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3ZGP

NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem

Summary for 3ZGP
Entry DOI10.2210/pdb3zgp/pdb
Related3ZG4
NMR InformationBMRB: 18911
DescriptorERFK/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 Keywordstransferase, transpeptidation, peptidoglycan biosynthesis, antibiotic resistance
Biological sourceENTEROCOCCUS FAECIUM
Total number of polymer chains1
Total formula weight15049.68
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 citationLecoq, 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: 23574509
DOI: 10.1021/cb4001603
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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