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TitleEvolution of carbapenemase activity in the class C beta-lactamase ADC-1.
Journal, issue, pagesMbio, Vol. 16, Page e0018525-e0018525, Year 2025
Publish dateJan 12, 2025 (structure data deposition date)
AuthorsStewart, N.K. / Toth, M. / Bhattacharya, M. / Smith, C.A. / Vakulenko, S.B.
External linksMbio / PubMed:40293226
MethodsX-ray diffraction
Resolution1.3 - 1.8 Å
Structure data

PDB-9mtu:
Crystal structure of apo-ADC-1 beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-9mtv:
Crystal structure of an apo-ADC-1 triple mutant
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-9mtw:
Crystal structure of ADC-1-ertapenem complex
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NO3:
NITRATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1RG:
(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 / medication, antibiotic*YM

PDB-1b93:
METHYLGLYOXAL SYNTHASE FROM ESCHERICHIA COLI

Source
  • acinetobacter baumannii (bacteria)
KeywordsHYDROLASE / beta-lactamase / class C / apo-enzyme / HYDROLASE/INHIBITOR / ANTIBIOTIC / ertapenem / acyl-enzyme complex / HYDROLASE-INHIBITOR / ANTIBIOTIC complex

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