7LLH

KPC-2 F72Y mutant with acylated imipenem

Summary for 7LLH

Entry DOI	10.2210/pdb7llh/pdb
Descriptor	Carbapenem-hydrolyzing beta-lactamase KPC, (5R)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-3-[(2-{[(E)-iminomethyl]amino}ethyl)sulfanyl]-4,5-dihydro-1H-pyrrole-2-carbox ylic acid (3 entities in total)
Functional Keywords	kpc, carbapenemase, beta-lactamase, hydrolase, antibiotic resistance, enzyme, beta-lactam, antibiotics, hydrolase-antibiotic complex, hydrolase/antibiotic
Biological source	Klebsiella pneumoniae
Total number of polymer chains	2
Total formula weight	55848.90
Authors	Furey, I.,Palzkill, T.,Sankaran, B.,Hu, L.,Prasad, B.V.V. (deposition date: 2021-02-03, release date: 2021-05-26, Last modification date: 2023-10-18)
Primary citation	Furey, I.M.,Mehta, S.C.,Sankaran, B.,Hu, L.,Prasad, B.V.V.,Palzkill, T. Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 beta-lactamase. J.Biol.Chem., 296:100799-100799, 2021 Cited by PubMed: 34022225 DOI: 10.1016/j.jbc.2021.100799 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation