5ul8 | pdb_00005ul8

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

spinqualitylabelsall models 5ul8, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ul8 is a 1 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLKPC_KLEPN Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency. Publication Abstract from PubMed Carbapenem-resistant Enterobacteriaceae are resistant to most beta-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A beta-lactamase. Here, we present the first product complex crystal structures of KPC-2 with beta-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 beta-lactamase, elucidating the product release mechanism of these enzymes in general. Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).,Pemberton OA, Zhang X, Chen Y J Med Chem. 2017 Apr 17. doi: 10.1021/acs.jmedchem.7b00158. PMID:28388065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

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