7LK8
Crystal structure of KPC-2 T215P mutant
Summary for 7LK8
Entry DOI | 10.2210/pdb7lk8/pdb |
Descriptor | Beta-lactamase, SODIUM ION (3 entities in total) |
Functional Keywords | kpc, carbapenemase, beta-lactamase, hydrolase, antibiotic resistance, enzyme, beta-lactam, antibiotics |
Biological source | Klebsiella pneumoniae |
Total number of polymer chains | 2 |
Total formula weight | 55191.01 |
Authors | Furey, I.,Palzkill, T.,Sankaran, B.,Hu, L.,Prasad, B.V.V. (deposition date: 2021-02-01, 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 (1.43 Å) |
Structure validation
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