3N8S
Crystal Structure of BlaC-E166A covalently bound with Cefamandole
Summary for 3N8S
Entry DOI | 10.2210/pdb3n8s/pdb |
Descriptor | Beta-lactamase, PHOSPHATE ION, (2R)-2-[(1R)-1-{[(2R)-2-hydroxy-2-phenylacetyl]amino}-2-oxoethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid, ... (4 entities in total) |
Functional Keywords | penicillin binding protein, beta-lactam covalent adduct, hydrolase-antibiotic complex, hydrolase/antibiotic |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 28869.15 |
Authors | Tremblay, L.W.,Blanchard, J.S. (deposition date: 2010-05-28, release date: 2010-11-24, Last modification date: 2017-11-08) |
Primary citation | Tremblay, L.W.,Xu, H.,Blanchard, J.S. Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants. Biochemistry, 49:9685-9687, 2010 Cited by PubMed: 20961112DOI: 10.1021/bi1015088 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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