4N9K
crystal structure of beta-lactamse PenP_E166S in complex with cephaloridine
Summary for 4N9K
Entry DOI | 10.2210/pdb4n9k/pdb |
Related | 4N92 4N9L |
Descriptor | Beta-lactamase, 5-METHYL-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID (3 entities in total) |
Functional Keywords | hydrolase, hydrolase-antibiotic complex, hydrolase/antibiotic |
Biological source | Bacillus licheniformis |
Cellular location | Cell membrane; Lipid-anchor (Probable): P00808 |
Total number of polymer chains | 2 |
Total formula weight | 60252.37 |
Authors | |
Primary citation | Pan, X.,Wong, W.,He, Y.,Jiang, Y.,Zhao, Y. Perturbing the General Base Residue Glu166 in the Active Site of Class A beta-Lactamase Leads to Enhanced Carbapenem Binding and Acylation Biochemistry, 53:5414-5423, 2014 Cited by PubMed: 25020031DOI: 10.1021/bi401609h PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
Download full validation report