4N9L
crystal structure of beta-lactamse PenP_E166S in complex with meropenem
Summary for 4N9L
Entry DOI | 10.2210/pdb4n9l/pdb |
Related | 4N92 4N9K |
Descriptor | Beta-lactamase, (2S,3R,4S)-4-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-3,4-dihydro-2H-pyrrole-5-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 | 60342.49 |
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 (2.3 Å) |
Structure validation
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