7LNL
Crystal structure of KPC-2 S70G/T215P mutant with hydrolyzed imipenem
Summary for 7LNL
| Entry DOI | 10.2210/pdb7lnl/pdb |
| Descriptor | Carbapenem-hydrolyzing beta-lactamase KPC, (2R)-2-[(2S,3R)-1,3-bis(oxidanyl)-1-oxidanylidene-butan-2-yl]-4-(2-methanimidamidoethylsulfanyl)-2,3-dihydro-1H-pyrrole -5-carboxylic 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 | 57264.54 |
| Authors | Furey, I.,Palzkill, T.,Sankaran, B.,Hu, L.,Prasad, B.V.V. (deposition date: 2021-02-07, 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: 34022225DOI: 10.1016/j.jbc.2021.100799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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