4Q8I

Crystal Structure of beta-lactamase from M.tuberculosis covalently complexed with Tebipenem

Summary for 4Q8I

• Entry DOI: 10.2210/pdb4q8i/pdb
• Related: 4QB8
• Descriptor: Beta-lactamase, (4R,5S)-3-(1-(4,5-dihydrothiazol-2-yl)azetidin-3-ylthio)-5-((2S,3R)-3-hydroxy-1-oxobutan-2-yl)-4-methyl-4,5- dihydro-1H-pyrrole-2-carboxylic acid, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: betalactam, betalactamase, carbapenem, tebipenem, tebipenem pivoxil, 3-layer sandwich, dd-peptidase/beta-lactamase superfamily, hydrolase-antibiotic complex, hydrolase/antibiotic
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane; Lipid-anchor (Potential): P9WKD3
• Total number of polymer chains: 1
• Total formula weight: 29166.24

Authors

Hazra, S.,Blanchard, J. (deposition date: 2014-04-27, release date: 2014-08-20, Last modification date: 2023-09-20)

• Primary citation: Hazra, S.,Xu, H.,Blanchard, J.S.; Tebipenem, a new carbapenem antibiotic, is a slow substrate that inhibits the beta-lactamase from Mycobacterium tuberculosis.; Biochemistry, 53:3671-3678, 2014; PubMed: 24846409; DOI: 10.1021/bi500339j

Experimental method

X-RAY DIFFRACTION (1.901 Å)