7LLB
Crystal structure of KPC-2 S70G/T215P mutant with hydrolyzed meropenem
Summary for 7LLB
| Entry DOI | 10.2210/pdb7llb/pdb |
| Descriptor | Carbapenem-hydrolyzing beta-lactamase KPC, (2S,3R)-2-[(2S,3R)-1,3-bis(oxidanyl)-1-oxidanylidene-butan-2-yl]-4-[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfan yl-3-methyl-2,3-dihydro-1H-pyrrole-5-carboxylic acid (3 entities in total) |
| Functional Keywords | carbapenemase, beta-lactamase, hydrolase, antibiotic resistance, beta-lactam, antibiotics |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 2 |
| Total formula weight | 56719.94 |
| 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: 34022225DOI: 10.1016/j.jbc.2021.100799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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