5UL8

Apo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolution

Summary for 5UL8

Entry DOI	10.2210/pdb5ul8/pdb
Related	5UJ3 5UJ4
Descriptor	Carbapenem-hydrolyzing beta-lactamase KPC, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywords	beta-lactamase, carbapenemase, klebsiella, high-resolution, hydrolase
Biological source	Klebsiella pneumoniae
Total number of polymer chains	1
Total formula weight	31282.98
Authors	Pemberton, O.A.,Chen, Y. (deposition date: 2017-01-24, release date: 2017-04-26, Last modification date: 2024-10-23)
Primary citation	Pemberton, O.A.,Zhang, X.,Chen, Y. Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2). J. Med. Chem., 60:3525-3530, 2017 Cited by PubMed Abstract: Carbapenem-resistant Enterobacteriaceae are resistant to most β-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A β-lactamase. Here, we present the first product complex crystal structures of KPC-2 with β-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine β-lactamase, elucidating the product release mechanism of these enzymes in general. PubMed: 28388065 DOI: 10.1021/acs.jmedchem.7b00158 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.15 Å)

Structure validation